Updated on 2025/04/01

Information

 

写真a

 
KAKUTA YOSHIMITSU
 
Organization
Faculty of Agriculture Department of Bioscience and Biotechnology Professor
School of Agriculture Department of Bioresource and Bioenvironment(Concurrent)
Graduate School of Bioresource and Bioenvironmental Sciences Department of Bioscience and Biotechnology(Concurrent)
Title
Professor
Contact information
メールアドレス
Profile
My main research is structural biology about sulfotransferase and glycosyltransferase.
External link

Degree

  • PhD.

Research Interests・Research Keywords

  • Research theme: Structural biology about sulfotransferase and glycosyltransferase

    Keyword: Structural biology, Crystallograpy, Sulfotransferase, Glycosyltransferase

    Research period: 1995.4

Awards

  • 農芸化学奨励賞

    2007.3   日本芸農芸化学会   X線結晶構造解析による酵素反応の分子機構に関する研究

Papers

  • Structural insights into lab-coevolved RNA-RBP pairs and applications of synthetic riboswitches in cell-free system. Reviewed

    Fukunaga K, Teramoto T, Nakashima M, Ohtani T, Katsuki R, Matsuura T, Yokobayashi Y, Kakuta Y

    Nucleic acids research   53 ( 6 )   2025.3   ISSN:0305-1048

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    Authorship:Last author, Corresponding author   Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1093/nar/gkaf212

    PubMed

  • The strategy used by naïve anti-PEG antibodies to capture flexible and featureless PEG chains Reviewed

    Liu, YW; Mori, T; Ito, Y; Kuroki, K; Hayashi, S; Kohda, D; Shimizu, T; Ishida, T; Roffler, SR; Kaneko, MK; Kato, Y; Arimori, T; Teramoto, T; Takemura, K; Ishibashi, K; Katayama, Y; Maenaka, K; Kakuta, Y; Kitao, A; Mori, T

    JOURNAL OF CONTROLLED RELEASE   380   396 - 403   2025.4   ISSN:0168-3659 eISSN:1873-4995

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    Authorship:Corresponding author   Language:English   Publishing type:Research paper (scientific journal)   Publisher:Journal of Controlled Release  

    Polyethylene glycol (PEG) is widely used as a standard stealth polymer, although the induction of anti-PEG antibodies and consequent effects have drawn attention in recent years. To date, several anti-PEG antibodies induced by PEG-modified proteins via the T cell-dependent (TD) pathway, in which affinity maturation occurs, have been reported. In contrast, structures of the naïve anti-PEG antibodies before affinity maturation have not been described in the literature. Here, to understand the details of the naïve anti-PEG antibodies capturing PEG, we studied a naïve anti-PEG antibody induced by a PEG-modified liposome in the absence of affinity maturation via the T cell-independent (TI) pathway. The mutation levels, structures as well as in vitro and in silico binding properties of TI and TD anti-PEG antibodies were compared. The TI anti-PEG antibody showed no mutation and a low binding affinity toward PEG, meanwhile, it allowed PEG chain sliding and weak interaction with the terminal group. Furthermore, the naïve anti-PEG antibodies may obtain high affinities by forming tunnel structures via minimal mutations. This research provides new insights into polymer–antibody interactions, which can facilitate the development of novel stealth polymers that can avoid antibody induction.

    DOI: 10.1016/j.jconrel.2025.02.001

    Web of Science

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  • Substrate binding and catalytic mechanism of UDP-α-D-galactofuranose: β-galactofuranoside β-(1→5)-galactofuranosyltransferase GfsA Reviewed

    Oka, T; Okuno, A; Hira, D; Teramoto, T; Chihara, Y; Hirata, R; Kadooka, C; Kakuta, Y

    PNAS NEXUS   3 ( 11 )   pgae482   2024.11   eISSN:2752-6542

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    UDP-α-D-galactofuranose (UDP-Galf): β-galactofuranoside β-(1→5)-galactofuranosyltransferase, known as GfsA, is essential in synthesizing β-(1→5)-galactofuranosyl oligosaccharides that are incorporated into the cell wall of pathogenic fungi. This study analyzed the structure and function of GfsA from Aspergillus fumigatus. To provide crucial insights into the catalytic mechanism and substrate recognition, the complex structure was elucidated with manganese (Mn2+), a donor substrate product (UDP), and an acceptor sugar molecule (β-galactofuranose). In addition to the typical GT-A fold domain, GfsA has a unique domain formed by the N and C termini. The former interacts with the GT-A of another GfsA, forming a dimer. The active center that contains Mn2+, UDP, and galactofuranose forms a groove structure that is highly conserved in the GfsA of Pezizomycotina fungi. Enzymatic assays using site-directed mutants were conducted to determine the roles of specific active-site residues in the enzymatic activity of GfsA. The predicted enzyme–substrate complex model containing UDP-Galf characterized a specific β-galactofuranosyltransfer mechanism to the 5'-OH of β-galactofuranose. Overall, the structure of GfsA in pathogenic fungi provides insights into the complex glycan biosynthetic processes of fungal pathogenesis and may inform the development of novel antifungal therapies.

    DOI: 10.1093/pnasnexus/pgae482

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  • Crystal structure of activating sulfotransferase SgdX2 involved in biosynthesis of secondary metabolite sungeidine Reviewed International journal

    #Takahiro Mori, @Takamasa Teramoto, @Yoshimitsu Kakuta

    Biochemical and Biophysical Research Communications   2024.4

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    DOI: 10.1016/j.bbrc.2024.149891

  • A new type of sulfation reaction: C-sulfonation for α,β-unsaturated carbonyl groups by a novel sulfotransferase SULT7A1 Reviewed

    Kurogi, K; Sakakibara, Y; Hashiguchi, T; Kakuta, Y; Kanekiyo, M; Teramoto, T; Fukushima, T; Bamba, T; Matsumoto, J; Fukusaki, E; Kataoka, H; Suiko, M

    PNAS NEXUS   3 ( 3 )   pgae097 - pgae097   2024.2   eISSN:2752-6542

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    Cytosolic sulfotransferases (SULTs) are cytosolic enzymes that catalyze the transfer of sulfonate group to key endogenous compounds, altering the physiological functions of their substrates. SULT enzymes catalyze the O-sulfonation of hydroxy groups or N-sulfonation of amino groups of substrate compounds. In this study, we report the discovery of C-sulfonation of α,β-unsaturated carbonyl groups mediated by a new SULT enzyme, SULT7A1, and human SULT1C4. Enzymatic assays revealed that SULT7A1 is capable of transferring the sulfonate group from 3′-phosphoadenosine 5′-phosphosulfate to the α-carbon of α,β-unsaturated carbonyl-containing compounds, including cyclopentenone prostaglandins as representative endogenous substrates. Structural analyses of SULT7A1 suggest that the C-sulfonation reaction is catalyzed by a novel mechanism mediated by His and Cys residues in the active site. Ligand-activity assays demonstrated that sulfonated 15-deoxy prostaglandin J2 exhibits antagonist activity against the prostaglandin receptor EP2 and the prostacyclin receptor IP. Modification of α,β-unsaturated carbonyl groups via the new prostaglandin-sulfonating enzyme, SULT7A1, may regulate the physiological function of prostaglandins in the gut. Discovery of C-sulfonation of α,β-unsaturated carbonyl groups will broaden the spectrum of potential substrates and physiological functions of SULTs.

    DOI: 10.1093/pnasnexus/pgae097

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  • Crystal structure of mango α1,3/α1,4-fucosyltransferase elucidates unique elements that regulate Lewis a-dominant oligosaccharide assembly Reviewed International journal

    Takahiro Okada, Takamasa Teramoto, Hideyuki Ihara, Yoshitaka Ikeda, Yoshimitsu Kakuta

    Glycobiology   2024.2

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    DOI: https://doi.org/10.1093/glycob/cwae015

  • Crystal structure of tick tyrosylprotein sulfotransferase reveals the activation mechanism of the tick anticoagulant protein madanin Reviewed International journal

    Misa Yoshimura, Takamasa Teramoto, Hirai Asano, Yuka Iwamoto, Mariko Kondo, Etsuko Nishimoto, Yoshimitsu Kakuta

    J Biol Chem.   2024.2

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    DOI: https://doi.org/10.1016/j.jbc.2024.105748

    Repository Public URL: https://hdl.handle.net/2324/7173532

  • Disassembly and reassembly of the non-conventional thermophilic C-phycocyanin Reviewed International journal

    Hung Khac Nguyen, Takuo Minato, Takamasa Teramoto, Seiji Ogo, Yoshimitsu Kakuta, Ki-Seok Yoon

    Journal of Bioscience and Bioengineering   2024.1

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    DOI: https://doi.org/10.1016/j.jbiosc.2023.12.015

  • Non-conventional octameric structure of C-phycocyanin Reviewed International journal

    Takuo Minato, Takamasa Teramoto, Naruhiko Adachi, Nguyen Khac Hung, Kaho Yamada, Masato Kawasaki, Masato Akutsu, Toshio Moriya, Toshiya Senda, Seiji Ogo, Yoshimitsu Kakuta, Ki-Seok Yoon

    Communications biology   4 ( Article number: 1238 )   2021.10

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    DOI: 10.1038/s42003-021-02767-x

  • Minimal protein-only RNase P structure reveals insights into tRNA precursor recognition and catalysis Reviewed International journal

    @Takamasa Teramoto, #Takeshi Koyasu, @Naruhiko Adachi, @Masato Kawasaki, @Toshio Moriya, @Tomoyuki Numata, @Toshiya Senda, @Yoshimitsu Kakuta

    The Journal of Biological Chemistry   297 ( 3 )   2021.9

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    Ribonuclease P (RNase P) is an endoribonuclease that catalyzes the processing of the 5' leader sequence of precursor tRNA (pre-tRNA). Ribonucleoprotein RNase P and protein-only RNase P (PRORP) in eukaryotes have been extensively studied, but the mechanism by which a prokaryotic nuclease recognizes and cleaves pre-tRNA is unclear. To gain insights into this mechanism, we studied homologs of Aquifex RNase P (HARPs), thought to be enzymes of approximately 23 kDa comprising only this nuclease domain. We determined the cryo-EM structure of Aq880, the first identified HARP enzyme. The structure unexpectedly revealed that Aq880 consists of both the nuclease and protruding helical (PrH) domains. Aq880 monomers assemble into a dimer via the PrH domain. Six dimers form a dodecamer with a left-handed one-turn superhelical structure. The structure also revealed that the active site of Aq880 is analogous to that of eukaryotic PRORPs. The pre-tRNA docking model demonstrated that 5' processing of pre-tRNAs is achieved by two adjacent dimers within the dodecamer. One dimer is responsible for catalysis, and the PrH domains of the other dimer are responsible for pre-tRNA elbow recognition. Our study suggests that HARPs measure an invariant distance from the pre-tRNA elbow to cleave the 5' leader sequence, which is analogous to the mechanism of eukaryotic PRORPs and the ribonucleoprotein RNase P. Collectively, these findings shed light on how different types of RNase P enzymes utilize the same pre-tRNA processing.

    DOI: 10.1016/j.jbc.2021.101028.

  • Structural Insight Into the Recognition of Pathogen-Derived Phosphoglycolipids by C-type Lectin Receptor DCAR Reviewed International journal

    Zakaria Omahdi, #Yuto Horikawa, Masamichi Nagae, Kenji Toyonaga, Akihiro Imamura, Koichi Takato, Takamasa Teramoto, Hideharu Ishida, Yoshimitsu Kakuta, Sho Yamasaki

    The Journal of Biological Chemistry   2020.3

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    DOI: 10.1074/jbc.RA120.012491

  • Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1. Reviewed International journal

    Tanaka S, Nishiyori T, Kojo H, Otsubo R, Tsuruta M, Kurogi K, Liu MC, Suiko M, Sakakibara Y, Kakuta Y

    Scientific Reports   2017.8

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    DOI: 10.1038/s41598-017-07141-8.

  • A rationally engineered yeast pyruvyltransferase Pvg1p introduces sialylation-like properties in neo-human-type complex oligosaccharide. Reviewed International journal

    Yujiro Higuchi, Yoshinaga S, Tateno H, Hirabaysshi J, Nakakita S, Kenakiyo M, Kakuta Y, Takegawa K

    Scientific Reports   ( 6 )   2016.5

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    DOI: 10.1038/srep26349.

  • The crystal structure of novel chondroitin lyase ODV-E66, a baculovirus envelope protein Reviewed International journal

    Kawaguchi Y, Sugiura N, Kimata K, Kimura M, Kakuta Y

    FEBS Letters   2013.12

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  • Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction Reviewed International journal

    Teramoto T, Fujikawa Y, Kawaguchi Y, Kurogi K, Soejima M, Adachi R, Nakanishi Y, Mishiro-Sato E, Liu MC, Sakakibara Y, Suiko M, Kimura M, Kakuta Y

    Nature Communications   2013.3

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    ヒトタンパク質チロシン硫酸転移酵素が、ターゲットとなるタンパク質を硫酸化修飾するメカニズムを明らかにするために、この酵素とターゲットタンパク質が結合している状態の立体構造を、X線結晶構造解析により原子レベルで決定しました。
     その結果、この酵素は二量体を形成し、その二量体の間につくられる奥深い溝の部分でターゲットとなるタンパク質のチロシン残基部分を結合して、その部分で特異的に硫酸基をつけていることがわかりました。また、硫酸化修飾を受ける部分は、特徴的なL字型に90度折れ曲がっていました。この構造が決定されたことにより、これまで謎であったターゲットとなるタンパク質の選別方法が明らかになりました。
     その選別方法とは、「ターゲットとなるタンパク質の柔軟性の違い」と、「電荷による相互作用」の2つによるものでした。柔らかい構造をしたターゲットタンパク質は、タンパク質チロシン硫酸転移酵素の深い溝の奥に入り込み、さらに90度折れ曲がることで活性部位の適切な位置に結合して、硫酸化修飾をうけることができます。しかし、硬い構造をしたタンパク質は、この溝に入ることができず、硫酸化修飾をうけることができません。また、タンパク質チロシン硫酸転移酵素が持つ深い溝表面には、プラスの電荷が多数準備されていて、ターゲットとなるタンパク質のマイナスの電荷を持った部分を特異的に認識します。
    このように、タンパク質チロシン硫酸転移酵素は、様々なタンパク質の柔軟性の違いと電荷による相互作用の両方を用いて、硫酸基をつけるターゲットタンパク質を選別していることが明らかになりました。
     タンパク質チロシン硫酸転移酵素の立体構造が明らかになり、そのターゲットとなるタンパク質の認識方法がわかったことで、この酵素に対する阻害剤の開発が可能になりました。硫酸基がつくことによるタンパク質の機能変化は、様々な生命現象に関わっています。したがって、特異的な阻害剤が開発できれば、ウイルス感染に対する薬としての利用だけでなく、生体防御反応の制御など、新しいタイプの医薬品としての応用が期待できます。

    DOI: 10.1038

  • Glucuronyltransferase activity of KfiC from Escherichia coli strain K5 requires association of KfiA: KfiC and KfiA are essential enzymes for production of K5 polysaccharide, N-acetylheparosan. Reviewed International journal

    Sugiura N, Baba Y, Kawaguchi Y, Iwatani T, Suzuki K, Kusakabe T, Yamagishi K, Kimata K, Kakuta Y, Watanabe H.

    The Journal of Biological Chemistry   285 ( 3 )   2010.1

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  • On the similar spatial arrangement of active site residues in PAPS-dependent and phenolic sulfate-utilizing sulfotransferases. Reviewed International journal

    Teramoto T, Adachi R, Sakakibara Y, Liu MC, Suiko M, Kimura M, Kakuta Y.

    FEBS Lett.   2009.9

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  • Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate. Reviewed International journal

    Teramoto T, Sakakibara Y, Liu MC, Suiko M, Kimura M, Kakuta Y.

    Biochem Biophys Res Commun.   2009.5

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  • Structural basis for the broad range substrate specificity of a novel mouse cytosolic sulfotransferase--mSULT1D1. Reviewed International journal

    Teramoto T, Sakakibara Y, Liu MC, Suiko M, Kimura M, Kakuta Y.

    Biochem Biophys Res Commun.   2009.1

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  • Crystal structure of chondroitin polymerase from Escherichia coli K4. Reviewed International journal

    Osawa T, Sugiura N, Shimada H, Hirooka R, Tsuji A, Shirakawa T, Fukuyama K, Kimura M, Kimata K, Kakuta Y.

    Biochem Biophys Res Commun.   2009.1

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  • Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects. Reviewed International journal

    Takagi H, Kakuta Y, Okada T, Yao M, Tanaka I, Kimura M.

    Nature structural & molecular biology   12 ( 4 )   327 - 331   2005.4

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    DOI: 10.1038/nsmb911

  • Crystal structure of the alginate (poly alpha-l-guluronate) lyase from Corynebacterium sp. at 1.2 A resolution. Reviewed International journal

    Osawa T, Matsubara Y, Muramatsu T, Kimura M, Kakuta Y.

    The Journal of Molecular Biology   345 ( 5 )   1111 - 1118   2005.2

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    DOI: 10.1016/j.jmb.2004.10.081

  • The crystal structure of exonuclease RecJ bound to Mn2+ ion suggests how its characteristic motifs are involved in exonuclease activity. Reviewed International journal

    Yamagata A., Kakuta Y., Masui R., Fukuyama K.

    Proceedings of the National Academy of Sciences of the United States of America.   2002.4

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  • Crystal structure of sulfotransferase domain of human heparan sulfate N-deacetylase/N-sulfotransferase 1. Reviewed International journal

    Kakuta, Y., Sueyoshi, T., Negishi, M., and Pedersen, L.C.

    The Journal of Biological Chemistry   1999.1

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  • Conserved structural motifs of the sulfotransferase family. Reviewed International journal

    Kakuta, Y., Pedersen, L.C., Pedersen, L.G., and Negishi, M.

    Trends in Biochemical Sciences   1998.1

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  • Crystal structure of estrogen sulphotransferase. Reviewed International journal

    Kakuta Y, Pedersen LG, Carter CW, Negishi M, Pedersen LC.

    Nature structural biology   1997.11

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  • Taste receptor type 1 member 3 in osteoclasts regulates osteoclastogenesis via detection of glucose

    Yoshimura, A; Matsubara, T; Kodama, N; Kakuta, Y; Yasuda, K; Yoshida, R; Kaminuma, O; Hosomi, S; Shinkawa, H; Yuan, Q; Kawamoto, T; Kokabu, S

    JOURNAL OF BIOLOGICAL CHEMISTRY   301 ( 3 )   108273   2025.3   ISSN:00219258 eISSN:1083-351X

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    The taste system extends beyond the oral cavity, with various taste receptors found in extraoral organs. Mice deficient in the taste receptor type 1 (TAS1R) family member, TAS1R3, and fed a high-fat, high-sugar diet showed high bone mass without altering food consumption. However, the underlying mechanisms, including the cell types responsible for TAS1R3 expression, remain unclear. Here, we demonstrate the expression and function of TAS1R3 in osteoclasts, which are responsible for bone resorption. The expression of Tas1r3, but not Tas1r1 or Tas1r2, is evoked during osteoclast differentiation. Osteoclastogenesis-related genes were downregulated in TAS1R3-deficient mice, whereas the opposite phenotypes were elicited by TAS1R3 overexpression. Contrary to the common heterodimerization with TAS1R1 or TAS1R2, TAS1R3 formed a homodimer that functioned to detect glucose, enhance p38 phosphorylation, and induce osteoclastogenesis. These results provide novel insights into the role of TAS1R3 in bone metabolism and suggest that TAS1R3 may be a viable target for therapeutic agents in bone metabolic diseases.

    DOI: 10.1016/j.jbc.2025.108273

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  • KIF22 regulates mitosis and proliferation of chondrocyte cells

    Kawaue, H; Matsubara, T; Nagano, K; Ikedo, A; Rojasawasthien, T; Yoshimura, A; Nakatomi, C; Imai, Y; Kakuta, Y; Addison, WN; Kokabu, S

    ISCIENCE   27 ( 7 )   110151   2024.7   eISSN:2589-0042

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    Point mutations in KIF22 have been linked to spondyloepimetaphyseal dysplasia with joint laxity, type 2 (SEMDJL2). Skeletal features of SEMDJL2 include short stature and joint laxity. Mechanisms underlying these limb abnormalities are unknown. Here in this manuscript, we have investigated the function of KIF22 in chondrocytes. Quantitative PCR and immunostaining revealed that Kif22 was highly expressed in proliferating-zone growth-plate chondrocytes. Kif22 knockdown resulted in defective mitotic spindle formation and reduced cell proliferation. Forced expression of SEMDJL-associated mutant Kif22 constructs likewise induced abnormal mitotic spindle morphology and reduced proliferation. Mice expressing a KIF22 truncation mutant had shorter growth plates and shorter tibial bones compared to wild-type mice. These results suggest that KIF22 regulates mitotic spindle formation in proliferating chondrocytes thereby linking the stunted longitudinal bone growth observed in SEMDJL2 to failures of chondrocyte division.

    DOI: 10.1016/j.isci.2024.110151

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  • Orthogonality of α-Sulfoquinovosidase in Human Cells and Development of Its Fluorescent Substrate

    Yoshida, R; Kaguma, R; Kaneko, R; Matsuo, I; Yoritate, M; Hirai, G; Teramoto, T; Kakuta, Y; Minamihata, K; Kamiya, N; Nii, T; Kishimura, A; Mori, T; Katayama, Y

    SENSORS AND MATERIALS   36 ( 8 )   3227 - 3238   2024   ISSN:0914-4935

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    Human orthogonal enzymes (HOEs) do not show the same activities as the endogenous enzymes of human cells and thus are useful as amplification enzymes to detect antigen proteins in biological samples. Here, we evaluate a new HOE from Escherichia coli, α-sulfoquinovosidase (α-SQase). We confirmed that the activity of α-SQase did not exist in examined human cell lines, and thus it was applicable to live-cell enzyme-linked immunosorbent assay (ELISA) in which the antigen membrane protein on cells was detected without inactivating endogenous enzymes, a pretreatment required for cell ELISA using conventional amplification enzymes. Here, we also developed a fluorescent substrate for α-SQase whose active residue is located at the end of the narrow, deep pocket of the substrate recognition site. The designed methylumbelliferyl substrate with a hydroxyl benzyl alcohol linker showed a similar reactivity to the p-nitrophenol substrate, a good substrate for α-SQase.

    DOI: 10.18494/SAM4816

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  • Crystal structure of<i> Arabidopsis</i><i> thaliana</i> sulfotransferase SOT16 involved in glucosinolate biosynthesis

    Iwamoto, Y; Saito, S; Teramoto, T; Maruyama-Nakashita, A; Kakuta, Y

    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS   677   149 - 154   2023.10   ISSN:0006-291X eISSN:1090-2104

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    Glucosinolates (GSLs), a class of secondary metabolites found in Brassicaceae plants, play important roles in plant defense and contribute distinct flavors and aromas when used as food ingredients. Following tissue damage, GSLs undergo enzymatic hydrolysis to release bioactive volatile compounds. Understanding GSL biosynthesis and enzyme involvement is crucial for improving crop quality and advancing agriculture. Plant sulfotransferases (SOTs) play a key role in the final step of GSL biosynthesis by transferring sulfate groups to the precursor molecules. In the present study, we investigated the enzymatic reaction mechanism and broad substrate specificity of Arabidopsis thaliana sulfotransferase AtSOT16, which is involved in GSL biosynthesis, using crystal structure analysis. Our analysis revealed the specific catalytic residues involved in the sulfate transfer reaction and supported the hypothesis of a concerted acid-base catalytic mechanism. Furthermore, the docking models showed a strong correlation between the substrates with high predicted binding affinities and those experimentally reported to exhibit high activity. These findings provide valuable insights into the enzymatic reaction mechanisms and substrate specificity of GSL biosynthesis. The information obtained in this study may contribute to the development of novel strategies for manipulating GSL synthesis pathways in Brassica plants and has potential agricultural applications.

    DOI: 10.1016/j.bbrc.2023.08.020

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  • Crystal structure of Arabidopsis thaliana sulfotransferase SOT16 involved in glucosinolate biosynthesis Reviewed International journal

    #Yuka Iwamoto, @Seira Saito, @Takamasa Teramoto, @Akiko Maruyama-Nakashita, @Yoshimitsu Kakuta

    Biochemical and Biophysical Research Communications   677   149 - 154   2023.10

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    DOI: doi.org/10.1016/j.bbrc.2023.08.020

  • Crystal structure of a unique activating sulfotransferase SgdX2 involved in the sungeidine biosynthesis

    Mori, T; Teramoto, T; Kakuta, Y

    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES   79   C847 - C847   2023.8   ISSN:2053-2733

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  • Crystal structure of adenosine 5'-phosphosulfate kinase isolated from Archaeoglobus fulgidus Reviewed International journal

    #Tomoya Kawakami, @Takamasa Teramoto, @Yoshimitsu Kakuta

    Biochemical and Biophysical Research Communications   643   105 - 110   2023.2

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    DOI: 10.1016/j.bbrc.2022.12.081.

  • The crystal structure of mouse SULT2A8 reveals the mechanism of 7α-hydroxyl, bile acid sulfation Reviewed International journal

    Takamasa Teramoto, #Takeaki Nishio, Katsuhisa Kurogi, Yoichi Sakakibara, Yoshimitsu Kakuta

    Biochemical and Biophysical Research Communications   562   15 - 20   2021.7

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    DOI: 10.1016/j.bbrc.2021.04.113

  • Pentatricopeptide repeats of protein-only RNase P use a distinct mode to recognize conserved bases and structural elements of pre-tRNA Reviewed International journal

    Takamasa Teramoto, Kipchumba J Kaitany, Yoshimitsu Kakuta, Makoto Kimura, Carol A Fierke, Traci M Tanaka Hall

    Nucleic Acids Res   48 ( 21 )   11815 - 11826   2020.12

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    シロイヌナズナのProtein-only RNase P 1 (PRORP1)は、PPRドメインを用いて前駆体tRNAを認識するエンドリボヌクレアーゼであり、ヌクレアーゼドメインを用いてpre-tRNAから5′-leader配列を除去する触媒作用を持つ。PRORP1がtRNAを認識するメカニズムを解明するために、我々は、PPRドメインとtRNAPとの複合体の結晶構造を2.85Åの分解能で決定した。PRORP1のPPRドメインは、tRNAの構造的に保存されたエルボー領域に構造特異的に結合していた。PRORP1のPPRドメインによるtRNAの認識様式は、リボヌクレオプロテインRNase PによるtRNAの認識と類似しており、tRNA認識する上で収束進化した結果であると考察される。

    DOI: 10.1093/nar/gkaa627

  • Biochemical and structural characterization of a thermostable Dps protein with His-type ferroxidase centers and outer metal-binding sites Reviewed International journal

    Minato, Takuo; Teramoto, Takamasa; Kakuta, Yoshimitsu; Ogo, Seiji; Yoon, Ki-Seok

    FEBS Open Bio   2020.3

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    DOI: 10.1002/2211-5463.12837

  • Evaluation of the Influence of Halogenation on the Binding of Bisphenol A to the Estrogen-Related Receptor γ Reviewed International journal

    Keitaro Suyama, Shuhei Kaneko, Hitoshi Kesamaru, Xiaohui Liu, Ayami Matsushima, Yoshimitsu Kakuta, Takashi Okubo, Kazumi Kasatani, Takeru Nose

    Chemical Research in Toxicology   2020.2

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    DOI: 10.1021/acs.chemrestox.9b00379

  • Functional implication of archaeal homologues of human RNase P protein pair Pop5 and Rpp30. Reviewed International journal

    Hamasaki M, Hazeyama K, Iwasaki F, Ueda T, Nakashima T, Kakuta Y, Kimura M

    Journal of Biochemistry   159 ( 1 )   31 - 40   2016.1

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    DOI: 10.1093/jb/mvv067

  • Mutation of the gene encoding the ribonuclease P RNA in the hyperthermophilic archaeon Thermococcus kodakarensis causes decreased growth rate and impaired process. Reviewed International journal

    Ueda T, Ishino S, Suematsu K, Nakashima T, Kakuta Y, Kimura M

    Biochem Biophys Res Commun.   468 ( 4 )   660 - 665   2015.12

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    DOI: 10.1016/j.bbrc.2015.11.012.

  • Archaeal ribonuclease P proteins have potential for biotechnological applications where precise hybridization of nucleic acids is needed. Reviewed International journal

    Miyanoshita M, Nakashima T, Kakuta Y, Kimura M

    Biosci Biotechnol Biochem.   79 ( 12 )   2014 - 2017   2015.6

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    DOI: 10.1080/09168451.2015.1058699

  • On archaeal homologs of the human RNase P proteins Pop5 and Rpp30 in the hyperthermophilic archaeon Thermococcus kodakarensis. Reviewed International journal

    Suematsu K, Ueda T, Nakashima T, Kakuta Y, Kimura M

    Biosci Biotechnol Biochem.   2015.2

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    DOI: 10.1080/09168451.2014.1003130

  • Enhancement of RNA annealing and strand displacement found in archaeal ribonuclease P proteins is conserved in Escherichia coli protein C5 and yeast protein Rpr2 Reviewed International journal

    Furutani T, Hazeyama K, Ueda T, Tomita S, Imai T, Gao X, Nakashima T, Kakuta Y, Kimura M

    Biosci Biotechnol Biochem.   2014.10

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    DOI: 10.1080/09168451

  • Characterization of putative toxin/antitoxin systems in Vibrio parahaemolyticus. Reviewed International journal

    Hino M, Zhang J, Takagi H, Miyoshi T, UchiumiT, Nakashima T, Kakuta Y, Kimura M

    J Appl Microbiol.   2014.9

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    DOI: 10.1111

  • Pentatricopeptide repeat motifs in the processing enzyme PRORP1 in Arabidopsis thaliana play a crucial role in recognition of nucleotide bases at TψC loop in precursor tRNAs Reviewed International journal

    Imai T, Nakamura T, Maeda T, Nakayama K, Gao X, Nakashima T, Kakuta Y, Kimura M

    Biochem Biophys Res Commun   2014.8

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    DOI: 10.1016

  • Tamavidin 2-HOT, a highly thermostable biotin-binding protein Reviewed International journal

    Takakura Y, Suzuki J, Oka N, Kakuta Y

    Journal of Biotechnology   2014.1

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  • Characterization of the peripheral structures of archaeal RNase P RNA from Pyrococcus horikoshii OT3 Reviewed International journal

    Ueda T, Yamaguchi H, Miyanoshita M, Nakashima T, Kakuta Y, Kimura M

    The Journal of Biochemistry   2014.1

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    DOI: 10.1093/jb/mvt092

  • Extra-structural elements in the RNA recognition motif in archaeal Pop5 play a crucial role in the activation of RNase P RNA from Pyrococcus horikoshii OT3 Reviewed International journal

    Hazeyama K, Ishihara M, Ueda T, Nishimoto E, Nakashima T, Kakuta Y, Kimura M

    Biochemical and Biophysical Research Communications   2013.11

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  • A distinct binding mode of archaeal ribonuclease P proteins to RNA Reviewed International journal

    Ishihara M, Nishimoto E, Yamashita S, Kakuta Y, Kimura M

    Biosci Biotechnol Biochem. 76(12):2335-7.   2012.12

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  • Single-molecular enzymatic elongation of hyaluronan polymers visualized by high-speed atomic force microscopy Reviewed International journal

    Mori T, Hirose A, Hagiwara T, Ohtsuka M, Kakuta Y, Kimata K, Okahata Y

    J Am Chem Soc. 134(50):20254-7.   2012.12

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    DOI: 10.1021

  • The structural basis for a coordinated reaction catalyzed by a bifunctional glycosyltransferase in chondroitin biosynthesis. Reviewed International journal

    Sobhany M, Kakuta Y, Sugiura N, Kimata K, Negishi M

    J Biol Chem. 287(43):36022-8.   2012.10

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  • Structural basis for catalytic activity of a silkworm Delta-class glutathione transferase Reviewed International journal

    Yamamoto K, Usuda K, Kakuta Y, Kimura M, Higashiura A, Nakagawa A, Aso Y, Suzuki M

    Biochim Biophys Acta. 2012 Oct;1820(10):1469-74.   2012.10

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  • Loss-of-function mutation in bi-functional marine bacterial sialyltransferase Reviewed International journal

    Kajiwara H, Katayama S, Kakuta Y, Okino N, Ito M, Mine T, Yamamoto T

    Biosci Biotechnol Biochem. 2012;76(9):1639-44.   2012.9

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  • Crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose Reviewed International journal

    Chaen K, Noguchi J, Omori T, Kakuta Y, Kimura M

    Biochem Biophys Res Commun. 2012 424(3):508-11.   2012.8

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  • Kinetics of iterative carbohydrate transfer to polysaccharide catalyzed by chondroitin polymerase on a highly sensitive flow-type 27 MHz quartz-crystal microbalance Reviewed International journal

    Mori T, Kodera T, Yoshimine H, Kakuta Y, Sugiura N, Kimata K, Okahata Y

    Chemistry. 2012 ;18(24):7388-93.   2012.6

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  • Thermodynamic analysis of a multifunctional RNA-binding protein, PhoRpp38, in the hyperthermophilic archaeon Pyrococcus horikoshii OT3. Reviewed International journal

    Oshima K, Nakashima T, Kakuta Y, Tsumoto K, Kimura M

    Biosci Biotechnol Biochem. 2012;76(6):1252-5.   2012.6

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  • Crystallization and X-ray diffraction analysis of chondroitin lyase from baculovirus: envelope protein ODV-E66. Reviewed International journal

    Kawaguchi Y, Sugiura N, Onishi M, Kimata K, Kimura M, and Kakuta Y.

    Acta. Crystallogr. Sect F   68   2012.2

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  • Crystal structure of sulfotransferase STF9 from Mycobacterium avium. Reviewed International journal

    Hossain MM, Moriizumi Y, Tanaka S, Kimura M, Kakuta Y.

    Mol Cell Biochem.   ( 361 )   2012.2

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  • Structural modeling of RNase P RNA from the hyperthermophilic archaeon Pyrococcus horikoshii OT3. Reviewed International journal

    Zwieb C, Nakao Y, Nakashima H, Takagi H, Goda S, Andersen E.S, Kakuta Y, and Kimura M.

    Biochem Biophys Res Commun.   in press   2011.10

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  • Molecular cloning, expression, and functional analysis of a predicted sulfotransferase STF9 from Mycobacterium avium. Reviewed International journal

    Hossain MM, Moriizumi Y, Tanaka S, Kimura M, Kakuta Y.

    Mol Cell Biochem.   350 ( (1-2) )   2011.10

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  • Crystallographic survey of active sites of an unclassified glutathione transferase from Bombyx mori.

    Kakuta Y, Usuda K, Nakashima T, Kimura M, Aso Y, Yamamoto K.

    Biochim Biophys Acta.   in press   2011.7

  • The Contribution of Peripheral Stem-Loops to the Catalytic Activity of Archaeal RNase P RNA from Pyrococcus horikoshii OT3. Reviewed International journal

    Hara T, Terada A, Yamaguchi H, Nakashima T, Kakuta Y, Kimura M.

    Biosci Biotechnol Biochem.   75(4)   2011.5

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  • Crystal structure of the branching enzyme I (BEI) from Oryza sativa L with implications for catalysis and substrate binding. Reviewed International journal

    Noguchi J, Chaen K, Vu NT, Akasaka T, Shimada H, Nakashima T, Nishi A, Satoh H, Omori T, Kakuta Y, Kimura M.

    Glycobiology   ( 8 )   2011.4

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  • The structural mechanism of the inhibition of archaeal RelE toxin by its cognate RelB antitoxin. Reviewed International journal

    Shinohara M, Guo JX, Mori M, Nakashima T, Takagi H, Nishimoto E, Yamashita S, Tsumoto K, Kakuta Y, Kimura M.

    Biochem Biophys Res Commun.   400   2010.9

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  • Structure of the newly found green turtle egg-white ribonuclease. Reviewed International journal

    Katekaew S, Kuaprasert B, Torikata T, Kakuta Y, Kimura M, Yoneda K, Araki T.

    Acta. Crystallogr. Sect F   66   2010.6

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  • Zebrafish as a model for the study of the phase II cytosolic sulfotransferases. Reviewed International journal

    Liu TA, Bhuiyan S, Liu MY, Sugahara T, Sakakibara Y, Suiko M, Yasuda S, Kakuta Y, Kimura M, Williams FE, Liu MC.

    Curr. Drug Metab.   6   2010.6

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  • Expression and functional analysis of a predicted AtsG arylsulfatase identified from Mycobacterium tuberculosis genomic data. Reviewed International journal

    Hossain MM, Kawarabayasi Y, Kimura M, Kakuta Y.

    J Biochem.   146 ( 6 )   2009.12

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  • Crystal structure of alpha/beta-galactoside alpha2,3-sialyltransferase from a luminous marine bacterium, Photobacterium phosphoreum Reviewed International journal

    Iwatani T, Okino N, Sakakura M, Kajiwara H, Takakura Y, Kimura M, Ito M, Yamamoto T, Kakuta Y.

    FEBS Lett.   2009.6

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  • Mechanistic insights into the hydrolysis and synthesis of ceramide by neutral ceramidase. Reviewed International journal

    Inoue T, Okino N, Kakuta Y, Hijikata A, Okano H, Goda HM, Tani M, Sueyoshi N, Kambayashi K, Matsumura H, Kai Y, Ito M.

    J Biol Chem.   2009.4

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  • Tamavidins--novel avidin-like biotin-binding proteins from the Tamogitake mushroom. Reviewed International journal

    Takakura Y, Tsunashima M, Suzuki J, Usami S, Kakuta Y, Okino N, Ito M, Yamamoto T.

    FEBS J.   2009.3

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  • Structure of an archaeal homolog of the human protein complex Rpp21-Rpp29 that is a key core component for the assembly of active ribonuclease P. Reviewed International journal

    Honda T, Kakuta Y, Kimura K, Saho J, Kimura M.

    J Mol Biol.   2008.12

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  • Tributyltin-binding protein type 1 has a distinctive lipocalin-like structure and is involved in the excretion of tributyltin in Japanese flounder, Paralichthys olivaceus. Reviewed International journal

    Satone H, Oshima Y, Shimasaki Y, Tawaratsumida T, Oba Y, Takahashi E, Kitano T, Kawabata S, Kakuta Y, Honjo T.

    Aquat Toxicol.   2008.12

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  • Biochemical and Crystallographic Characterization of the Starch Branching Enzyme I (BEI) from Oryza sativa L. Reviewed International journal

    Vu NT, Shimada H, Kakuta Y, Nakashima T, Ida H, Omori T, Nishi A, Satoh H, Kimura M.

    Biosci Biotechnol Biochem.   2008.11

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  • Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase. Reviewed International journal

    Teramoto T, Sakakibara Y, Inada K, Kurogi K, Liu MC, Suiko M, Kimura M, Kakuta Y.

    FEBS Lett.   2008.11

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  • The Chondroitin Polymerase K4CP and the Molecular Mechanism of Selective Bindings of Donor Substrates to Two Active Sites. Reviewed International journal

    Sobhany M, Kakuta Y, Sugiura N, Kimata K, Negishi M.

    J Biol Chem.   2008.11

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  • Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase Reviewed International journal

    Noguchi J, Hayashi Y, Baba Y, Okino N, Kimura M, Ito M, Kakuta Y.

    Biochem Biophys Res Commun.   2008.9

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  • ERRgamma tethers strongly bisphenol A and 4-alpha-cumylphenol in an induced-fit manner. Reviewed

    Matsushima A, Teramoto T, Okada H, Liu X, Tokunaga T, Kakuta Y, Shimohigashi Y.

    Biochem Biophys Res Commun.   2008.8

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  • Crystal structure and functional analysis of an archaeal chromatin protein Alba from the hyperthermophilic archaeon Pyrococcus horikoshii OT3. Reviewed International journal

    Hada K, Nakashima T, Osawa T, Shimada H, Kakuta Y, Kimura M.

    Biosci Biotechnol Biochem.   2008.3

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  • Crystal structure of Vibrionaceae Photobacterium sp. JT-ISH-224 alpha-2,6-sialyltransferase in a ternary complex with donor product CMP and acceptor substrate lactose: catalytic mechanism and substrate recognition. Reviewed International journal

    Kakuta Y, Okino N, Kajiwara H, Ichikawa M, Takakura Y,Ito M, Yamamoto T

    Glycobiology   2008.1

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  • Crystal structure of an archaeal Ski2p-like protein from Pyrococcus horikoshii OT3. Reviewed International journal

    Zhang X, Nakashima T, Kakuta Y, Yao M, Tanaka I, Kimura M.

    Protein Sci.   2008.1

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  • Structural Evidence for Endocrine Disruptor Bisphenol A Binding to Human Nuclear Receptor ERR{gamma} Reviewed International journal

    Matsushima A, Kakuta Y, Teramoto T, Koshiba T, Liu X, Okada H, Tokunaga T, Kawabata SI, Kimura M, Shimohigashi Y.

    J Biochem (Tokyo)   2007.10

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  • Klotho-related Protein Is a Novel Cytosolic Neutral beta-Glycosylceramidase. Reviewed International journal

    Hayashi Y, Okino N, Kakuta Y, Shikanai T, Tani M, Narimatsu H, Ito M.

    J Biol Chem.   2007.10

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  • Crystal Structure of Tapes japonica Lysozyme with Substrate Analogue: STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND MANIFESTATION OF ITS CHITINASE ACTIVITY ACCOMPANIED BY QUATERNARY STRUCTURAL CHANGE. Reviewed International journal

    Goto T, Abe Y, Kakuta Y, Takeshita K, Imoto T, Ueda T.

    J Biol Chem.   2007.9

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  • Purification, crystallization and preliminary crystallographic characterization of the alpha 2,6-sialyltransferase from Photobacterium sp. JT-ISH-224. Reviewed International journal

    Okino N, Kakuta Y, Kajiwara H, Ichikawa M, Takakura Y, Ito M, Yamamoto T.

    Acta Crystallogr Sect F Struct Biol Cryst Commun.   2007.8

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  • Crystal structures of the Nicotiana glutinosa ribonuclease NT in complex with nucleoside monophosphates. Reviewed International journal

    Kawano S, Kakuta Y, Nakashima T, Kimura M.

    J Biochem (Tokyo).   2006.9

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  • A fifth protein subunit Ph1496p elevates the optimum temperature for the ribonuclease P activity from Pyrococcus horikoshii OT3 Reviewed International journal

    Fukuhara H, Kifusa M, Watanabe M, Terada A, Honda T, Numata T, Kakuta Y, Kimura M.

    J Biochem (Tokyo)   2006.5

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  • Crystal structure of protein Ph1481p in complex with protein Ph1877p of archaeal RNase P from Pyrococcus horikoshii OT3: implication of dimer formation of the holoenzyme Reviewed International journal

    Kawano S, Nakashima T, Kakuta Y, Tanaka I, Kimura M

    J. Mol Biol.   2006.3

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  • Crystal Structure of a Ribonuclease P Protein Ph1601p from Pyrococcus horikoshii OT3: An Archaeal Homologue of Human Nuclear Ribonuclease P Protein Rpp21 Reviewed International journal

    Kakuta Y, Ishimatsu I, Numata T, Kimura K, Yao M, Tanaka I, Kimura M.

    Biochemistry   44 ( 36 )   12086 - 12093   2005.9

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    DOI: 10.1021/bi050738z

  • Crystal structure of Escherichia coli YfhJ protein, a member of the ISC machinery involved in assembly of iron-sulfur clusters. Reviewed International journal

    Shimomura Y, Takahashi Y, Kakuta Y, Fukuyama K.

    Proteins.   60 ( 3 )   566 - 569   2005.8

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    DOI: 10.1002/prot.20481

  • Overproduction, purification and preliminary X-ray diffraction analysis of a sulfotransferase from Mycobacterium tuberculosis H37Rv. Reviewed International journal

    Tanaka S, Moriizumi Y, Kimura M, Kakuta Y.

    Acta Crystallograph Sect F Struct Biol Cryst Commun.   61   33 - 35   2005.1

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    DOI: 10.1107/S1744309104022328

  • Crystal structure of archaeal ribonuclease P protein Ph1771p from Pyrococcus horikoshii OT3: an archaeal homolog of eukaryotic ribonuclease P protein Rpp29. Reviewed International journal

    Numata T, Ishimatsu I, Kakuta Y, Tanaka I, Kimura M.

    RNA.   10 ( 9 )   1423 - 1432   2004.9

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    DOI: 10.1261/rna.7560904

  • Amino acids conserved at the C-terminal half of the ribonuclease T2 family contribute to protein stability of the enzymes. Reviewed International journal

    Kimura K, Numata T, Kakuta Y, Kimura M.

    Biosci Biotechnol Biochem.   68 ( 8 )   1748 - 1757   2004.8

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    DOI: 10.1271/bbb.68.1748

  • Crystal structure of the regulatory subunit of archaeal initiation factor 2B (aIF2B) from hyperthermophilic archaeon Pyrococcus horikoshii OT3: a proposed structure of the regulatory subcomplex of eukaryotic IF2B Reviewed International journal

    Kakuta Y, Tahara M, Maetani S, Yao M, Tanaka I, Kimura M.

    Biochem. Biophys. Res. Commun   319 ( 3 )   725 - 732   2004.7

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    DOI: 10.1016/j.bbrc.2004.05.045

  • Crystal structure of the ribonuclease P protein Ph1877p from hyperthermophilic archaeon Pyrococcus horikoshii OT3. Reviewed International journal

    Takagi H, Watanabe M, Kakuta Y, Kamachi R, Numata T, Tanaka I, Kimura M.

    Biochem Biophys Res Commun.   319 ( 3 )   787 - 794   2004.7

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    DOI: 10.1016/j.bbrc.2004.05.055

  • Overproduction, crystallization and preliminary X-ray diffraction analysis of probable ATP sulfurylase from Thermus thermophilus HB8 Reviewed International journal

    Taguchi Y, Hoseki J, Kakuta Y, Fukuyama K.

    Acta. Crystallogr. D   2003.9

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  • Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH: Implication for NADPH and Substrate Recognition Reviewed International journal

    Shimomura Y, Kakuta Y, Fukuyama K.

    J. Bacteriol.   185 ( 14 )   4211 - 4218   2003.7

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    DOI: 10.1128/JB.185.14.4211.4218.2003

  • Crystal Structures of the Ribonuclease MC1 Mutants N71T and N71S in Complex with 5’-GMP: Structural Basis for Alterations in Substrate Specificity Reviewed International journal

    Numata T, Suzuki A, Kakuta Y, Kimura K, Yao M, Tanaka I, Yoshida Y, Ueda T, Kimura M.

    Biochemistry   42 ( 18 )   5270 - 5278   2003.5

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    DOI: 10.1021/bi034103g

  • Heparan sulphate N-sulphotransferase activity: reaction mechanism and substrate recognition Reviewed International journal

    Kakuta Y, Li L, Pedersen LC, Pedersen LG, Negishi M.

    Biochem. Soc. Trans   2003.4

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  • Atomic resolution structures of oxidized [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus in two crystal forms: systematic distortion of [4Fe-4S] cluster in the protein. Reviewed International journal

    Fukuyama K., Okada T., Kakuta Y., Takahashi Y.

    Journal of Molecular Biology   2002.1

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  • Crystal Structure of Rat Apo-Heme Oxygenase-1 (HO-1): Mechanism of Heme Binding in HO-1 Inferred from Structural Comparison of the Apo and Heme Complex Forms. Reviewed International journal

    Sugishima M., Sakamoto H., Kakuta Y., Omata Y., Hayashi S., Noguchi M., Fukuyama K.

    Biochemistry   2002.1

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  • Guanine binding site of the Nicotiana glutinosa ribonuclease NW revealed by X-ray crystallography. Reviewed International journal

    Kawano S., Kakuta Y., and Kimura M.

    Biochemistry   41 ( 51 )   15195 - 15202   2002.1

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    DOI: 10.1021/bi0262471

  • Overexpression, purification and characterization of RecJ protein from Thermus thermophilus HB8 and its core domain. Reviewed International journal

    Yamagata A., Masui R., Kakuta Y., Kuramitsu S., Fukuyama K.

    Nucleic Acids Research   2001.1

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  • Crystal structure of the Escherichia coli Fdx, an Adrenodoxin-type Ferredoxin Involved in the Assembly of Iron-Sulfur Clusers. Reviewed International journal

    Kakuta Y., Horio T., Takahashi Y., and Fukuyama K.

    Biochemistry   2001.1

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  • Structure-Function Modeling of the Interactions of N-Alkyl-N-hydroxyanilines with Rat Hepatic Aryl Sulfotransferase IV. Reviewed International journal

    King RS, Sharma V., Pedersen L.C., Kakuta Y., Negishi M., and Duffel MW.

    Chem Res Toxicol   2000.1

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  • Crystal structure of rat heme oxygenase-1 in complex with heme. Reviewed International journal

    Sugishima M., Omata Y., Kakuta Y., Sakamoto H., Noguchi M., and Fukuyama K.

    FEBS Letter   2000.1

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  • Substrate gating confers steroid specificity to estrogen sulfotransferase. Reviewed International journal

    Petrotchenko EV, Doerflein ME, Kakuta Y., Pedersen L.C., and Negishi M.

    The Journal of Biological Chemistry   1999.1

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  • 3'-Phosphoadenosine 5'-phosphosulfate binding site of flavonol 3-sulfotransferase srudied by affinity chromatography and 31P NMR. Reviewed International journal

    Marsolais, F., Laviolette, M., Kakuta, Y., Negishi, M., Pedersen, L.C., Auger, M., and Varin, L.

    Biochemistry   1999.1

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    Language:English   Publishing type:Research paper (scientific journal)  

  • A quantum mechanical study of the transfer of biological sulfate. Reviewed International journal

    Bartolotti, L., Kakuta, Y., Pedersen, L.C., Negishi, M., and Pedersen, L.G.

    Theochem-Journal of Molecular Structure.   1999.1

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    Language:English   Publishing type:Research paper (scientific journal)  

  • Crystal structure of human catecholamine sulfotransferase. Reviewed International journal

    Bidwell LM, McManus ME, Gaedigk A, Kakuta Y., Negishi M., Pedersen L., and Martin JL.

    Journal of Molecular Biology   1999.1

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    Language:English   Publishing type:Research paper (scientific journal)  

  • A role of Lys614 in the sulfotransferase activity of human heparan sulfate N-deacetylase/N-sulfotranferase. Reviewed International journal

    Sueyoshi, T., Kakuta, Y., Pedersen, L.C., Frances, E.W., Pedersen, L.G., and Negishi, M.

    FEBS Letter   1998.1

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    Language:English   Publishing type:Research paper (scientific journal)  

  • Mouse steroid sulfotransferases: substrate specificity and preliminary X-ray crystallographic analysis. Reviewed International journal

    Kakuta, Y., Pedersen, L.C., Chae, K., Song, W., Leblanc, D., London, R., Carter, C.W., and Negishi, M.

    Biochemical Pharmacology   1998.1

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    Language:English   Publishing type:Research paper (scientific journal)  

  • The sulfuryl transfer mechanism: Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis. Reviewed International journal

    Kakuta, Y., Petrotchenko E.V., Pedersen, L.C., and Negishi, M.

    The Journal of Biological Chemistry   1998.1

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    Language:English   Publishing type:Research paper (scientific journal)  

  • Glycine-15 in the bend between two alpha-helices can explain the thermostability of DNA binding protein HU from Bacillus stearothermophilus. Reviewed International journal

    Kawamura S, Kakuta Y, Tanaka I, Hikichi K, Kuhara S, Yamasaki N, Kimura M.

    Biochemistry.   35 ( 4 )   1195 - 1200   1996.1

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1021/bi951581l

  • 1H NMR study on substituent distribution of cellulose diacetate Reviewed International journal

    Hikichi, K., Kakuta, Y., and Katoh, T.

    Polymer Journal   1995.1

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    Language:English   Publishing type:Research paper (scientific journal)  

  • 13C-NMR relaxation study on mobility of the DNA-binding arm of HU. Reviewed International journal

    Kakuta Y, Hojo H, Aimoto S, Tanaka I, Hikichi K.

    J Biochem (Tokyo).   1994.11

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    Language:English   Publishing type:Research paper (scientific journal)  

  • Development of a Linker with an Enhanced Stability for the Preparation of Peptide Thioesters and Its Application to the Synthesis of Stable-Isotope-Labelled HU-Type DNA-Binding Protein Reviewed International journal

    Hojo H., Kwon Y.,Kakuta Y.,Tsuda S.,Tanaka I.,Hikichi K., and Aimoto S.

    Bull. Chem. Soc. Jpn   1993.9

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    Language:English   Publishing type:Research paper (scientific journal)  

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MISC

  • リボヌクレアーゼP(RNase P)の多様性・構造基盤と分子進化 Reviewed

    @寺本岳大,#児安剛志、@角田佳充

    バイオサイエンスとインダストリー   2023.5

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    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)  

  • Crystal structure of endocrine-disrupting chemical bisphenol A and estrogen-related receptor γ Reviewed

    Ayami Matsushima, Takamasa Teramoto, Yoshimitsu Kakuta

    The Journal of Biochemistry   2022.1

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    Language:English   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)  

    DOI: https://doi.org/10.1093/jb/mvab145

  • リボヌクレアーゼP(RNase P)の多様性とその構造基盤 Reviewed

    @寺本岳大,#児安剛志、@角田佳充

    生化学(日本生化学会)   2021.12

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    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)  

    DOI: doi:10.14952/SEIKAGAKU.2021.930857

  • 古細菌リボヌクレアーゼP構成タンパク質の結晶構造解析

    角田佳充、木村 誠

    日本結晶学会誌   2007.9

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    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)  

  • ヘパラン硫酸スルホトランスフェラーゼの構造生物学

    角田佳充、Lars C. Pedersen、根岸正彦

    蛋白質核酸酵素   2001.1

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    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)  

  • 【JBにおけるProtein Data Bank50年史】内分泌攪乱物質ビスフェノールAとエストロゲン関連受容体γの結晶構造(【50 years of Protein Data Bank in JB】Crystal structure of endocrine-disrupting chemical bisphenol A and estrogen-related receptor γ)

    Matsushima Ayami, Teramoto Takamasa, Kakuta Yoshimitsu

    The Journal of Biochemistry   171 ( 1 )   23 - 25   2022.1   ISSN:0021-924X

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    Language:English   Publisher:(公社)日本生化学会  

  • 植物リボヌクレアーゼの基質認識機構

    沼田 倫征、 河野 慎、 角田 佳充、 木村 誠

    化学と生物   2003.1

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    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)  

  • Structure and Function of Sulfotransferases

    Negishi, M., Pedersen, L.G., Petrotchenko, E., Shevtsov, S., Gorokho, A., Kakuta, Y., Pedersen, L.C.

    Archives of Biochemistry and Biophysics   2001.1

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    Language:English   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)  

  • スルホトランスフェラーゼの構造生物学

    角田佳充、Lars C. Pedersen, 根岸 正彦

    日本結晶学会誌   2000.9

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    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)  

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Professional Memberships

  • 日本生化学会

  • TIGG

  • 日本糖質学会

  • 日本生物物理学会

  • 日本結晶学会

  • 日本蛋白質科学会

  • 日本農芸化学会

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Committee Memberships

  • 日本生化学会九州支部   Councilor   Domestic

    2019.4 - 2021.3   

  • 日本糖質学会   Councilor   Domestic

    2017.1 - 2020.12   

  • 日本農芸化学会西日本支部   Organizer   Domestic

    2011.1 - Present   

  • 日本農芸化学会西日本支部   参与   Domestic

    2011.1 - 2020.12   

  • 日本農芸化学会西日本支部   Organizer   Domestic

    2011.1 - 2012.12   

  • 日本生化学会九州支部   Organizer   Domestic

    2007.11 - 2008.10   

  • 日本農芸化学会   代議員   Domestic

    2007.4 - 2008.3   

  • 日本農芸化学会西日本支部   Organizer   Domestic

    2003.1 - 2004.12   

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Research Projects

  • 吸血生物が持つ血液凝固阻害タンパク質活性化の分子メカニズム解明

    Grant number:24K09353  2024 - 2026

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 抗凝血・抗炎症ポリペプチドの硫酸化機構の解明

    Grant number:21K05384  2021 - 2023

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 翻訳後修飾を行う植物タンパク質チロシン硫酸転移酵素の立体構造解析

    Grant number:16K07273  2016 - 2018

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 真核微生物のステリルグルコシド代謝とその生理機能

    Grant number:15H04488  2015 - 2017

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (B)

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    Authorship:Coinvestigator(s)  Grant type:Scientific research funding

  • 前駆体tRNAプロセシング酵素の構造と機能の解明とその有効利用

    Grant number:15H04487  2015 - 2017

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (B)

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    Authorship:Coinvestigator(s)  Grant type:Scientific research funding

  • 宇宙環境を利用した高品質タンパク質結晶生成と精密立体構造の解析

    2009.10 - 2010.9

    Research commissions

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    Authorship:Principal investigator  Grant type:Other funds from industry-academia collaboration

  • スフィンゴ糖脂質代謝マシーナリの構造と機能及び応用に関する研究

    Grant number:21380066  2009 - 2011

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (B)

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    Authorship:Coinvestigator(s)  Grant type:Scientific research funding

  • 高効率な部位特異的硫酸化タンパク質生産法の開発

    2009

    JST シーズ発掘試験研究

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    Authorship:Principal investigator  Grant type:Contract research

  • リボ核タンパク質複合体酵素の作用機構に関する研究

    Grant number:19380060  2007 - 2009

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (B)

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    Authorship:Coinvestigator(s)  Grant type:Scientific research funding

  • 核内受容体ERRgammaを介したビスファノールAの低用量効果の解明

    Grant number:19201012  2007 - 2009

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (A)

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    Authorship:Coinvestigator(s)  Grant type:Scientific research funding

  • 硫酸転移酵素による多様な生体異物認識の立体構造基盤解明

    Grant number:19570106  2007 - 2008

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 新しいエンド型・エキソ型グリコサラミダーゼの構造と機能及び応用に関する研究

    Grant number:19380061  2007 - 2008

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (B)

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    Authorship:Coinvestigator(s)  Grant type:Scientific research funding

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Educational Activities

  • 大学院教育では、「生物機能分子化学I」「生物物理化学特論」の講義において、タンパク質の立体構造と機能の関係、立体構造決定法、立体構造情報解析法について概説している。
    学部教育では、「基礎生化学I」「生物化学I」「生物物理化学I」「生物物理化学II」の講義において、アミノ酸、タンパク質の精製法、タンパク質の構造と機能の関係などについて概説している。

Class subject

  • 生物物理化学特論

    2024.10 - 2024.12   Fall quarter

  • 生物化学I

    2024.10 - 2024.12   Fall quarter

  • 生物物理化学II

    2024.6 - 2024.8   Summer quarter

  • 科学英語

    2024.4 - 2025.3   Full year

  • 応用生命化学発展実験

    2024.4 - 2024.9   First semester

  • 生物機能分子化学Ⅱ

    2024.4 - 2024.9   First semester

  • 生物機能分子化学プロジェクト演習

    2024.4 - 2024.9   First semester

  • 基礎生化学I

    2024.4 - 2024.6   Spring quarter

  • 生物物理化学I

    2024.4 - 2024.6   Spring quarter

  • 生物物理化学特論

    2023.10 - 2023.12   Fall quarter

  • 生物物理化学特論

    2023.10 - 2023.12   Fall quarter

  • 生物化学I

    2023.10 - 2023.12   Fall quarter

  • 生物物理化学Ⅱ

    2023.6 - 2023.8   Summer quarter

  • 科学英語

    2023.4 - 2024.3   Full year

  • 応用生命化学発展実験

    2023.4 - 2023.9   First semester

  • 生物機能分子化学プロジェクト演習

    2023.4 - 2023.9   First semester

  • 生物機能分子化学Ⅱ

    2023.4 - 2023.9   First semester

  • 生物物理化学Ⅰ

    2023.4 - 2023.6   Spring quarter

  • 基礎生化学Ⅰ

    2023.4 - 2023.6   Spring quarter

  • 基礎生化学I

    2023.4 - 2023.6   Spring quarter

  • 生物物理化学特論

    2022.10 - 2022.12   Fall quarter

  • 生物化学Ⅰ

    2022.10 - 2022.12   Fall quarter

  • 生物物理化学特論

    2022.10 - 2022.12   Fall quarter

  • 生物化学I

    2022.10 - 2022.12   Fall quarter

  • 生物物理化学Ⅱ

    2022.6 - 2022.8   Summer quarter

  • 科学英語

    2022.4 - 2023.3   Full year

  • 応用生命化学発展実験

    2022.4 - 2022.9   First semester

  • 生物機能分子化学プロジェクト演習

    2022.4 - 2022.9   First semester

  • 生物機能分子化学Ⅱ

    2022.4 - 2022.9   First semester

  • 生物物理化学Ⅰ

    2022.4 - 2022.6   Spring quarter

  • 基礎生化学Ⅰ

    2022.4 - 2022.6   Spring quarter

  • 基礎生化学I

    2022.4 - 2022.6   Spring quarter

  • 生物化学I

    2021.10 - 2021.12   Fall quarter

  • 生物物理化学特論

    2021.10 - 2021.12   Fall quarter

  • 生物物理化学特論

    2021.10 - 2021.12   Fall quarter

  • 生物化学Ⅰ

    2021.10 - 2021.12   Fall quarter

  • 科学英語

    2021.4 - 2022.3   Full year

  • 生物機能分子化学プロジェクト演習

    2021.4 - 2021.9   First semester

  • 応用生命化学発展実験

    2021.4 - 2021.9   First semester

  • 基礎生化学

    2021.4 - 2021.9   First semester

  • 生物機能分子化学Ⅱ

    2021.4 - 2021.9   First semester

  • 生物物理化学

    2021.4 - 2021.9   First semester

  • 基礎生化学

    2021.4 - 2021.9   First semester

  • 生物化学

    2020.10 - 2021.3   Second semester

  • 生物化学

    2020.10 - 2021.3   Second semester

  • 専門英語

    2020.10 - 2021.3   Second semester

  • Life Engineering, Advanced Course Ⅹ

    2020.10 - 2020.12   Fall quarter

  • 生物物理化学特論

    2020.10 - 2020.12   Fall quarter

  • 構造生物学特論

    2020.10 - 2020.12   Fall quarter

  • 分析化学実験

    2020.4 - 2021.3   Full year

  • 応用生命化学実験

    2020.4 - 2021.3   Full year

  • 科学英語

    2020.4 - 2021.3   Full year

  • 生物物理化学

    2020.4 - 2020.9   First semester

  • 生物物理化学

    2020.4 - 2020.9   First semester

  • 基礎生化学

    2020.4 - 2020.9   First semester

  • 応用生命化学発展実験

    2020.4 - 2020.9   First semester

  • 生物機能分子化学Ⅱ

    2020.4 - 2020.9   First semester

  • 生物機能分子化学プロジェクト演習

    2020.4 - 2020.9   First semester

  • 生物物理化学特論

    2020.4 - 2020.9   First semester

  • 基礎生化学

    2020.4 - 2020.9   First semester

  • 生物化学

    2019.10 - 2020.3   Second semester

  • 生物化学

    2019.10 - 2020.3   Second semester

  • 応用生命化学発展実験

    2019.10 - 2020.3   Second semester

  • 学術英語3・個別テーマ

    2019.10 - 2020.3   Second semester

  • Life Engineering, Advanced Course Ⅹ

    2019.10 - 2019.12   Fall quarter

  • 構造生物学特論

    2019.10 - 2019.12   Fall quarter

  • 生物物理化学特論

    2019.10 - 2019.12   Fall quarter

  • 酵素化学特論

    2019.10 - 2019.12   Fall quarter

  • 応用生命化学実験

    2019.4 - 2020.3   Full year

  • 卒業研究(応用生命化学分野)

    2019.4 - 2020.3   Full year

  • 分析化学実験

    2019.4 - 2020.3   Full year

  • 科学英語

    2019.4 - 2020.3   Full year

  • 実地見学

    2019.4 - 2020.3   Full year

  • 応用生命化学発展実験

    2019.4 - 2020.3   Full year

  • 生物物理化学

    2019.4 - 2019.9   First semester

  • 応用生命化学実験

    2019.4 - 2019.9   First semester

  • 生物物理化学

    2019.4 - 2019.9   First semester

  • 実地見学(応用生命化学分野)

    2019.4 - 2019.9   First semester

  • 科学英語(応用生命化学分野)

    2019.4 - 2019.9   First semester

  • 基礎生化学

    2019.4 - 2019.9   First semester

  • 生物物理化学特論

    2019.4 - 2019.9   First semester

  • 生物機能分子化学プロジェクト演習

    2019.4 - 2019.9   First semester

  • 生物機能分子化学Ⅱ

    2019.4 - 2019.9   First semester

  • 応用生命化学発展実験

    2019.4 - 2019.9   First semester

  • 基礎生化学

    2019.4 - 2019.9   First semester

  • 生物化学実験

    2018.10 - 2019.3   Second semester

  • 生物化学

    2018.10 - 2019.3   Second semester

  • 生物化学

    2018.10 - 2019.3   Second semester

  • 生物物理化学特論

    2018.10 - 2018.12   Fall quarter

  • 構造生物学特論

    2018.10 - 2018.12   Fall quarter

  • 生体高分子学特論

    2018.4 - 2018.9   First semester

  • 生物物理化学

    2018.4 - 2018.9   First semester

  • 基礎生化学

    2018.4 - 2018.9   First semester

  • 生物物理化学

    2018.4 - 2018.9   First semester

  • 基礎生化学

    2018.4 - 2018.9   First semester

  • 生物化学

    2017.10 - 2018.3   Second semester

  • 生物化学

    2017.10 - 2018.3   Second semester

  • 酵素化学特論

    2017.10 - 2018.3   Second semester

  • 生体高分子学特論

    2017.10 - 2018.3   Second semester

  • 生物化学実験

    2017.10 - 2018.3   Second semester

  • 構造生物学特論

    2017.10 - 2017.12   Fall quarter

  • 修士論文

    2017.4 - 2018.3   Full year

  • 生物機能分子化学プロジェクト演習

    2017.4 - 2018.3   Full year

  • 生物機能分子化学特別研究第一

    2017.4 - 2018.3   Full year

  • 生物機能分子化学特別研究第二

    2017.4 - 2018.3   Full year

  • 生物物理化学

    2017.4 - 2017.9   First semester

  • 生物物理化学

    2017.4 - 2017.9   First semester

  • 基礎生化学

    2017.4 - 2017.9   First semester

  • 蛋白質化学特論

    2017.4 - 2017.9   First semester

  • 生体高分子学特論

    2017.4 - 2017.9   First semester

  • 基礎生化学

    2017.4 - 2017.9   First semester

  • 生物化学

    2016.10 - 2017.3   Second semester

  • 生物化学実験

    2016.10 - 2017.3   Second semester

  • 基礎生化学

    2016.4 - 2016.9   First semester

  • 生物物理化学

    2016.4 - 2016.9   First semester

  • 生体高分子学特論

    2016.4 - 2016.9   First semester

  • 応用生物科学概要

    2016.4 - 2016.9   First semester

  • 蛋白質化学特論

    2016.4 - 2016.9   First semester

  • Molecular Biology

    2016.4 - 2016.9   First semester

  • 生物化学

    2015.10 - 2016.3   Second semester

  • 応用生物科学概要

    2015.10 - 2016.3   Second semester

  • 生物化学実験

    2015.10 - 2016.3   Second semester

  • 基礎生化学

    2015.4 - 2015.9   First semester

  • 生体高分子学特論

    2015.4 - 2015.9   First semester

  • 応用生物科学概要

    2015.4 - 2015.9   First semester

  • 蛋白質化学特論

    2015.4 - 2015.9   First semester

  • Molecular Biology

    2015.4 - 2015.9   First semester

  • 生物化学

    2014.10 - 2015.3   Second semester

  • 応用生物科学概要

    2014.10 - 2015.3   Second semester

  • 生物化学実験

    2014.10 - 2015.3   Second semester

  • 基礎化学B

    2014.4 - 2014.9   First semester

  • 生体高分子学特論

    2014.4 - 2014.9   First semester

  • 応用生物科学概要

    2014.4 - 2014.9   First semester

  • 蛋白質化学特論

    2014.4 - 2014.9   First semester

  • Molecular Biology

    2014.4 - 2014.9   First semester

  • 応用生物科学概要

    2013.10 - 2014.3   Second semester

  • 生物化学

    2013.10 - 2014.3   Second semester

  • 生物化学実験

    2013.10 - 2014.3   Second semester

  • 生体高分子学特論

    2013.4 - 2013.9   First semester

  • 基礎化学B

    2013.4 - 2013.9   First semester

  • Molecular Biology

    2013.4 - 2013.9   First semester

  • 蛋白質化学特論

    2013.4 - 2013.9   First semester

  • 応用生物科学概要

    2013.4 - 2013.9   First semester

  • 応用生物科学概要

    2012.10 - 2013.3   Second semester

  • 生物化学

    2012.10 - 2013.3   Second semester

  • 生物化学実験

    2012.10 - 2013.3   Second semester

  • 応用生物科学概要

    2012.4 - 2012.9   First semester

  • 基礎化学B

    2012.4 - 2012.9   First semester

  • 生体高分子学特論

    2012.4 - 2012.9   First semester

  • 生物化学

    2011.10 - 2012.3   Second semester

  • 生物化学実験

    2011.10 - 2012.3   Second semester

  • 生体高分子学特論

    2011.4 - 2011.9   First semester

  • 基礎化学B

    2011.4 - 2011.9   First semester

  • 生物化学実験

    2010.10 - 2011.3   Second semester

  • 生物化学

    2010.10 - 2011.3   Second semester

  • 生体高分子学特論

    2010.4 - 2010.9   First semester

  • 生物化学実験

    2009.10 - 2010.3   Second semester

  • 生物化学

    2009.10 - 2010.3   Second semester

  • コアセミナー

    2009.4 - 2009.9   First semester

  • 生物化学実験

    2008.10 - 2009.3   Second semester

  • 生物化学

    2008.10 - 2009.3   Second semester

  • 生体高分子学特論

    2008.4 - 2008.9   First semester

  • 生物化学実験

    2007.10 - 2008.3   Second semester

  • 生物化学

    2007.10 - 2008.3   Second semester

  • 生体高分子特論

    2007.10 - 2008.3   Second semester

  • 生物化学

    2006.10 - 2007.3   Second semester

  • コアセミナー

    2006.4 - 2006.9   First semester

  • 蛋白質構造論

    2006.4 - 2006.9   First semester

  • 生物化学

    2005.10 - 2006.3   Second semester

  • 生物化学

    2004.10 - 2005.3   Second semester

  • 生物化学

    2003.10 - 2004.3   Second semester

  • 生物化学

    2002.10 - 2003.3   Second semester

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FD Participation

  • 2021.3   Role:Speech   Title:FD講演会「九州大学オンライン授業のグッドプラクティス 〜 リアルタイム型授業編〜」

    Organizer:[Undergraduate school/graduate school/graduate faculty]

  • 2020.12   Role:Participation   Title:大学の研究評価の現状と農学研究院の「部局独自の評価基準」案における業績分析

    Organizer:[Undergraduate school/graduate school/graduate faculty]

  • 2009.8   Role:Participation   Title:FD

    Organizer:[Undergraduate school/graduate school/graduate faculty]

  • 2006.9   Role:Participation   Title:不明

    Organizer:[Undergraduate school/graduate school/graduate faculty]

  • 2006.6   Role:Participation   Title:不明

    Organizer:[Undergraduate school/graduate school/graduate faculty]

  • 2003.7   Role:Participation   Title:不明

    Organizer:[Undergraduate school/graduate school/graduate faculty]

  • 2002.12   Role:Participation   Title:不明

    Organizer:[Undergraduate school/graduate school/graduate faculty]

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Visiting, concurrent, or part-time lecturers at other universities, institutions, etc.

  • 2018  長崎大学  Classification:Part-time lecturer  Domestic/International Classification:Japan 

Social Activities

  • 九州大学「世界に羽ばたく未来創成科学者育成プロジェクト(QFC‐SP)」

    2024.4

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 模擬講義「タンパク質・酵素の立体構造解析からわかること」

    大分県立上野丘高校  2023.12

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 九州大学「世界に羽ばたく未来創成科学者育成プロジェクト(QFC‐SP)」

    2023.4

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 九州大学「世界に羽ばたく未来創成科学者育成プロジェクト(QFC‐SP)」

    2022.4

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 九州大学「世界に羽ばたく未来創成科学者育成プロジェクト(QFC‐SP)」

    2021.8

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 九州大学「世界に羽ばたく未来創成科学者育成プロジェクト(QFC‐SP)」

    2020.8

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 出張講義

    西南学院高等学校  2019.11

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 九州大学「世界に羽ばたく未来創成科学者育成プロジェクト(QFC‐SP)」

    2019.8

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 九州大学「世界に羽ばたく未来創成科学者育成プロジェクト(FC‐SP)」

    2018.8

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 九州大学「世界に羽ばたく未来創成科学者育成プロジェクト(FC‐SP)」

    2017.8

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 九州大学「世界に羽ばたく未来創成科学者育成プロジェクト(FC‐SP)」

    2016.8

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 夏の学校

    高等学校の生物及び化学の教諭対象  2016.6

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • スーパーサイエンスハイスクール事業における蛋白質結晶学実験

    修猷館高校  2006.7

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 高校生受入プログラム

    長崎東高校  2005.7

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 高校生のための科学講演会

    都城市  2003.11

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 秋の学校(バイオインフォマティクス)

    高等学校の生物及び化学の教諭対象  2003.10

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    Audience:Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

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Media Coverage

  • マダニのたんぱく質、血の凝固を抑える仕組み解明 Newspaper, magazine

    日本経済新聞  2024.2

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    マダニのたんぱく質、血の凝固を抑える仕組み解明

  • チロシン硫酸転移酵素のメカニズム解明 Newspaper, magazine

    NHK、日本経済新聞、朝日新聞、西日本新聞、秋田魁新報、宮崎日日新聞、静岡新聞  2013.3

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    チロシン硫酸転移酵素のメカニズム解明

Travel Abroad

  • 2017.3

    Staying countory name 1:United States   Staying institution name 1:ハワイ大学

  • 2016.3

    Staying countory name 1:United States   Staying institution name 1:ハワイ大学

  • 2015.3

    Staying countory name 1:United States   Staying institution name 1:ハワイ大学

  • 2014.8

    Staying countory name 1:United States   Staying institution name 1:トレド大学とNIEHS/NIH

  • 2014.3

    Staying countory name 1:United States   Staying institution name 1:ハワイ大学

  • 2013.3

    Staying countory name 1:Philippines   Staying institution name 1:アテネオ・デ・マニラ大学

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