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分子・構造解析施設 准教授
五味知治(Gomi, Tomoharu)


経歴など研究活動の概要主な研究業績| 

1990 to date (as of 12/10/2005)

アデノシルホモシステインヒドロラーゼ
(S-Adenosylhomocysteine hydrolase)

  1. Catalytic mechanism of S-adenosylhomocysteine hydrolase: roles of His54, Asp130, Glu155, Lys185, and Aspl89.
    Yamada, T., Takata, Y., Komoto, J., Gomi, T., Ogawa, H., Fujioka, M., and Takusagawa, F.
    Int. J. Biochem. Cell Biol. 37, 2417-2435 (2005) [PubMed 16061414]
  2. Catalytic mechanism of S-adenosylhomocysteine hydrolase: Site-directed mutagenesis of Asp-130, Lys-185, Asp-189, and Asn-190.
    Takata, Y., Yamada, T., Huang, Y., Komoto, J., Gomi, T., Ogawa, H., Fujioka, M., and Takusagawa, F.
    J. Biol. Chem. 277, 22670-22676 (2002) [PubMed 11927587]
  3. Inhibition of S-adenosylhomocysteine hydrolase by acyclic sugar adenosine analogue D-eritadenine: Crystal structure of S-adenosylhomocysteine hydrolase complexed with D-eritadenine.
    Huang, Y., Komoto, J., Takata, Y., Powell, D. R., Gomi, T., Ogawa, H., Fujioka, M., and Takusagawa, F.
    J. Biol. Chem. 277, 7477-7482 (2002) [PubMed 11741948]
  4. Effects of site-directed mutagenesis on structure and function of S-adenosylhomocysteine hydrolase: Crystal structure of D244E mutant enzyme.
    Komoto, J., Huang, Y., Gomi, T., Ogawa, H., Takata, Y., Fujioka, M., and Takusagawa, F.
    J. Biol. Chem. 275, 32147-32156 (2000) [PubMed 10913437]
  5. Crystal structure of S-adenosylhomocysteine hydrolase from rat liver.
    Hu, Y., Komoto, J., Huang, Y., Gomi, T., Ogawa, H., Takata, Y., Fujioka, M., and Takusagawa, F.
    Biochemistry 38, 8323-8333 (1999) [PubMed 10387078]
  6. The role of cysteine 78 in fluorosulfonylbenzoyladenosine inactivation of rat liver S-adenosyl-homocysteine hydrolase.
    Aksamit, R. R., Backlund, P. S. Jr., Moos, M. Jr., Caryk, T,. Gomi, T., Ogawa, H., Fujioka, M., and Cantoni, G. L.
    J. Biol. Chem. 269, 4084-4091 (1994) [PubMed 8307967]
  7. Site-directed mutagenesis of rat liver S-adenosylhomocysteinase. Effect of conversion of aspartic acid 244 to glutamic acid on coenzyme binding.
    Gomi, T.,. Takata, Y,. Date, T,. Fujioka, M., Aksamit, R. R., Backlund, P. S., Jr., and Cantoni G. L.
    J. Biol. Chem. 265, 16102-16107 (1990) [PubMed 1975808]

メチル基転移酵素
(Methyltransferases)

  1. Catalytic mechanism of guanidinoacetate methyltransferase: crystal structures of guanidinoacetate methyltransferase ternary complexes.
    Komoto, J., Yamada, T., Takata, Y., Konishi, K., Ogawa, H., Gomi, T., Fujioka, M., and Takusagawa, F.
    Biochemistry 43, 14385-14394 (2004) [PubMed 15533043]
  2. Monoclinic guanidinoacetate methyltransferase and gadolinium ion-binding characteristics.
    Komoto, J., Takata, Y., Yamada, T., Konishi, K., Ogawa, H., Gomi, T., Fujioka, M., and Takusagawa, F.
    Acta Crystallogr D Biol Crystallogr. 59(Pt 9):1589-1596 (2003) [PubMed 12925789]
  3. Catalytic mechanism of glycine N-methyltransferase.
    Takata, Y., Huang, Y., Komoto, J., Yamada, T., Konishi, K., Ogawa, H., Gomi, T., Fujioka, M., amd Takusagawa, F.
    Biochemistry; 42(28):8394-8402 (2003) [PubMed 12859184]
  4. Crystal structure of guanidinoacetate methyltransferase from rat liver: a model structure of protein arginine methyltransferase.
    Komoto, J., Huang, Y., Takata, Y., Yamada, T., Konishi, K., Ogawa, H., Gomi, T., Fujioka, M., and Takusagawa, F.
    J. Mol. Biol. 320, 223-235 (2002) [PubMed 12079381]
  5. Mechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes.
    Huang, Y., Komoto, J., Konishi, K., Takata, Y., Ogawa, H., Gomi, T., Fujioka, M., and Takusagawa, F.
    J. Mol. Biol. 298, 149-162 (2000) [PubMed 10756111]
  6. Crystallization and preliminary X-ray diffraction studies of guanidinoacetate methyltransferase from rat liver.
    Komoto, J., Huang, Y., Hu, Y., Takata, Y, Konishi, K., Ogawa, H., Gomi, T., Fujioka, M., and Takusagawa, F.
    Acta Crystallogr. D Biol. Crystallogr. 55, 1928-1929 (1999) [PubMed 10531498]
  7. Structure, function, and physiological role of glycine N-methyltransferase.
    Ogawa, H., Gomi, T., Takusagawa, F., and Fujioka, M.
    Int. J. Biochem. Cell Biol. 30, 13-26 (1998) [PubMed 9597750]
  8. C1-transferase
    藤岡基二,五味知治
    「タンパク質化学 第4巻 酵素,4-2 トランスフェラーゼ」小橋恭一編,3-79,廣川書店,東京,1998
  9. グリシンメチルトランスフェラーゼ ― その特異な構造と機能
    藤岡基二,五味知治,小川宏文
    ビタミン 71, 463-473 (1997)
  10. Recombinant expression of rat glycine N-methyltransferase and evidence for contribution of NH2-terminal acetylation to co-operative binding of S-adenosylmethionine.
    Ogawa, H., Gomi, T., Takata, Y., Date, T., and Fujioka, M.
    Biochem. J. 327, 407-412 (1997) [PubMed 9359408]
  11. Rat liver 4S-benzo[a]pyrene-binding protein is distinct from glycine N-methyltransferase.
    Ogawa, H., Gomi, T., Imamura, T., Kobayashi, M., and Huh, N.
    Biochem. Biophys. Res. Commun. 233, 300-304 (1997) [PubMed 9144528]
  12. Guanidinoacetate methyltransferase. Identification of the S-adenosylmethionine-binding site by affinity labeling and site-directed mutagenesis.
    Konishi, K., Takata, Y., Gomi, T., Ogawa, H., and Fujioka, M.
    In Guanidino Compounds in Biology and Medicine:: 2, by De Deyn, P. P., Marescau, B., Qureshi, I. A., and Mori, A. (Eds.) 121-130, John Libbey & Company Ltd., London, 1997
  13. Crystal structure of glycine N-methyltransferase from rat liver.
    Fu, Z., Hu, Y., Konishi, K., Takata, Y., Ogawa, H., Gomi, T., Fujioka, M., and Takusagawa, F.
    Biochemistry 35, 11985-11993 (1996) [PubMed 8810903]
  14. Probing the S-adenosylmethionine-binding site of rat guanidinoacetate methyltransferase. Effect of site-directed mutagenesis of residues that are conserved across mammmalian non-nucleic acid methyltransferases.
    Hamahata, A., Takata, Y., Gomi, T., and Fujioka, M.
    Biochem. J. 317, 141-145 (1996) [PubMed 8694756]
  15. Rat guanidinoacetate methyltransferase. Effect of site-directed alteration of an aspartic acid residue that is conserved across most mammalian S-adenosylmethionine-dependent methyltransferases.
    Takata, Y,. Konishi, K., Gomi, T., and Fujioka, M.
    J. Biol. Chem. 269, 5537-5542 (1994) [PubMed 8119887]
  16. Mammalian glycine N-methyltransferases. Comparative kinetic and structural properties of the enzymes from human, rat, rabbit and pig livers.
    Ogawa, H., Gomi, T., and Fujioka, M.
    Comp. Biochem. Physiol. 106B: 601-611 (1993) [PubMed 8281755]
  17. Rat guanidinoacetate methyltransferase: mutation of amino acids within a common sequence motif of mammalian methyltransferase does not affect catalytic activity but alters proteolytic susceptibility.
    Gomi, T.,. Tanihara, K., Date, T., and Fujioka, M.
    Int. J. Biochem. 24, 1639-1649 (1992) [PubMed 1397491]
  18. Structure-function relationships of guanidinoacetate methyltransferase as revealed by chemical modification and site-directed mutagenesis of cysteine residues
    Fujioka, M., Takata, Y., Konishi, K., Gomi, T., and Ogawa, H.
    In Guanidino Compounds in Biology and Medicine, by De Deyn, P. P., Marescau, B., Stalon, V., and Qureshi, I. L. (Eds.) 159-164, John Libbery & Company Ltd., London, 1992.
  19. Recombinant rat guanidinoacetate methyltransferase: structure and function of the NH2-terminal region as deduced by limited proteolysis.
    Fujioka, M., Takata, Y., and Gomi, T.
    Arch. Biochem. Biophys. 285, 181-186 (1991) [PubMed 1990977]

その他(アミノ酸代謝酵素、歯周病菌毒素、酸素添加酵素)
(Other enzymes)

  1. Some biochemical and histochemical properties of human liver serine dehydratase.
    Kashii, T., Gomi, T., Oya, T., Ishii, Y., Oda, H., Maruyama, M., Kobayashi, M., Masuda, T., Yamazaki, M., Nagata, T., Tsukada, K., Nakajima, A., Tatsu, K., Mori, H., Takusagawa, F., Ogawa, H., and Pitot, H. C.
    Int. J. Biochem. Cell Biol. 37, 574-589 (2005) [PubMed 15618015]
  2. Deletion and purification studies to elucidate the structure of the Actinobacillus actinomycetemcomitans cytolethal distending toxin.
    Saiki, K., Gomi, T., and Konishi, K.
    J. Biochem. 136, 335-342 (2004) [PubMed 15598890]
  3. Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity.
    Sato, K., Nakamura, T., Mizuguchi, M., Miura, K., Tada, M., Aizawa, T., Gomi, T., Miyamoto, K., and Kawano, K.
    FEBS Letters 553, 232-238 (2003) [PubMed 14572630]
  4. Evidence for a dimeric structures of rat liver serine dehydratase.
    Ogawa, H., Gomi, T., Takusagawa, F., Masuda, T., Goto, T., Kana, T., Huh, N.-H.
    Int. J. Biochem. Cell Biol. 34, 533-543 (2002) [PubMed 11906824]
  5. Reconstitution and purification of cytolethal distending toxin of Actinobacillus actinomycetemcomitans.
    Saiki, K., Konishi, K., Gomi, T., Nishihara, T., and Yoshikawa, M.
    Microbiol. Immunol. 45, 497-506 (2001) [PubMed 11497226]
  6. Serine hydroxymethyltransferase and threonine aldolase: Are they identical?
    Ogawa, H., Gomi, T., and Fujioka, M.
    Int. J. Biochem. Cell Biol. 32, 289-301 (2000) [PubMed 10716626]
  7. Enzymatic properties of dipeptidyl aminopeptidase IV produced by the periodontal pathogen Porphyromonas gingivalis and its participation in virulence.
    Kumagai, Y., Konishi, K., Gomi, T., Yagishita, H., Yajima, A., and Yoshikawa, M.
    Infect. Immun. 68, 716-724 (2000) [PubMed 10639438]
  8. Laparotomy causes a transient induction of rat liver serine dehydratase mRNA.
    Ogawa, H., Kawamata, S., Gomi, T., Ansai, Y., and Karaki, Y.
    Arch. Biochem. Biophys. 316, 844-850 (1995) [PubMed 7864642]
  9. Identification of a lysine residue in the NADH-binding site of salicylate hydroxylase from Pseudomonas putida S-1
    Suzuki, K., Mizuguchi, M., Gomi, T., and Itagaki, E.
    J. Biochem. 117, 579-585 (1995) [PubMed 7629025]
  10. Intermediate and mechanism of hydroxylation of o-iodophenol by salicylate hydroxylase.
    Suzuki, K., Gomi, T., and Itagaki, E.
    J. Biochem. 109, 791-797 (1991) [PubMed 1917904]
  11. Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase.
    Suzuki, K., Gomi, T., Kaidoh, T., and Itagaki, E.
    J. Biochem. 109, 348-353 (1991) [PubMed 1864847]

男性ホルモン@大阪(androgen @ Osaka)
  1. Androgen receptor in human placental villi
    Hirota, K., Gomi, T., Kishimoto, R., Iguchi, M., Hayakawa, K., and Nakagawa, H.
    J. Biochem., 89, 153-160 (1981)
  2. A novel nuclear protein in rat ventral prostate: Androgen-dependent and age-related change
    Kishimoto, R., Gomi, T., Izaike, Y., Nagai, K., and Nakagawa, H.
    Biochim. Biophys. Acta, 718, 165-171 (1982)

P-450@金沢 (Mitochondrial P-450 @ Kanazawa)
  1. Purification of cytochrome P-450 from bovine adrenocortical mitochondria by an "Aniline-Sepharose" and properties
    Takemori, S., Suhara, K., Hashimoto, S., Hashimoto, M., Sato, H., Gomi, T., and Katagiri, M.
    Biochem. Biophys. Res. Commun., 63, 588-593 (1975)
  2. Purification and properties of cytochrome P-45011b from adrenocortical mitochondria
    Takemori, S., Sato, H., Gomi, T., Suhara, K., and Katagiri, M.
    Biochem. Biophys. Res. Commun., 67, 1151-1157 (1975)
  3. Characterization of purified cytochrome P-450SCC and P-45011b from bovine adrenocortical mitochondria
    Katagiri, M., Takemori, S., Itagaki, E., Suhara, K., Gomi, T., and Sato, H.
    in Iron and Copper Proteins Yasunobu, K. T., Mower, H. F., and Hayaishi, O. (Eds.) pp. 281-289, Plenum Press, New York (1976)
  4. Purification and immunochemical characterization of two adrenal cortex cytochrome P-450-proteins
    Suhara, K., Gomi, T., Sato, H., Itagaki, E.,Takemori, S., and Katagiri, M.
    Arch. Biochem. Biophys., 190, 290-299 (1978)
  5. Properties of an adrenal cytochrome P-450 (P-450SCC) for the side chain cleavage of cholesterol
    Takikawa, O., Gomi, T., Suhara, K., Itagaki, E., Takemori, S., and Katagiri, M.
    Arch. Biochem. Biophys., 190, 300-306 (1978)


経歴など研究活動の概要主な研究業績|