2001 Fiscal Year Final Research Report Summary
Characterization of different enzymes catalyzing oxidative deamination of amines
| Project/Area Number |
11694212
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
応用微生物学・応用生物化学
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| Research Institution | Yamaguchi University |
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Principal Investigator |
ADACHI Osao Faculty of Agr., Yamaguchi U., Prof., 農学部, 教授 (20027189)
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| Co-Investigator(Kenkyū-buntansha) |
TANIZAWA Katsuyuki Inst. Sci. Ind. Res., Osaka U., Prof., 産業科学研究所, 教授 (20133134)
TOYAMA Hirohide Faculty of Agr., Yamaguchi U., As/Prof., 農学部, 助教授 (60240884)
MATSUSHITA Kazunobu Faculty of Agr., Yamaguchi U., Prof., 農学部, 教授 (50107736)
HIROTA Shun Fac. Sci., Nagoya U., As/Prof, 理学部, 助手 (90283457)
HITORSU Ken Fac. Sci., Osaka City U., Prof., 理学部, 教授 (10047269)
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| Project Period (FY) |
1999 – 2001
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| Keywords | amine oxidase / amine dehydrogenase / quinone cofactors / quinoproteins |
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| Research Abstract |
The crystal structure of a quinohemoprotein amine dehydrogenase from Pseudomonas putida has been determined at .1.9A resolution. The enzyme comprises three non-identical subunits ; a four-domain A-subunit that harbors adi-heme cytochrome c, a seven-bladed B-propeller B-subunit that provides part of the active site, and a small G-subunit that contains a novel cross-linked. proteinous quinone cofactor, cysteine tryptophylquinone. More suprisingly, the catalytic G-subunit contains three additional chemical cross-links that encage the cysteine trytpphylquinone cofactor, involving a cysteine side chain bridged to either an Asp or Glu residue all in a hitherto unknown thicether bonding with a methylene carbon atom of acidic amino acid side chains. Thus, the structure of the 79-residue G-subunit is quite unusual, containing four internal cross-links in such a short polypeptide chain that would otherwise be difficult to fold into a globular structure.
Spermidine dehydrogenase from Citrobacter freundii and histamine dehydrogenase from Nocardioides simplex have also been crystallized for X-ray analysis, which may develop another new fields of quinoprotein chemistry. Furthermore, it is very much promising to have been succeeded in purification of cytokinin oxidase and amino-aldehyde dehydrogenase from plants sources.
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Research Products
(12 results)
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[Publications] Vandenberghe J, K. Kim, B. Devreese, A. Hacisalihoglu, H. Iwabuki, T. Okajima, S. Kuroda, O. Adachi J, A. Jongejan, J. A. Duine, K. Tanizawa, and J. Van Beeumen: "The Covalent Structure of the Small Subunit from Pseudomonas putida Amine Dehydrogenase Reveals the Presence of Three Novel Types of Internal Cross-Linkages, All Involving Cysteine in a Thio-Ether Bond"J. Biol. Chem. 276. 42923-42931 (2001)
Description
「研究成果報告書概要(欧文)」より
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[Publications] S. Datta, Y. Mori, K. Takagi, K. Kawaguchi, Z. W. Chen, T. Okajima, S. Kuroda, T. Ikeda, K. Kano, K. Tanizawa, and F. S. Mathews: "Structure of a Quinohemoprotein Amine Dehydrogenase with an Uncommon Redox Cofactor and Highly Unusual Crosslinking"Proc. Natl. Acad. Sci. U.S.A. 98. 14268-14273 (2001)
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「研究成果報告書概要(欧文)」より
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[Publications] Atsuko Satoh, Jong-Keun Kim, Ikuko Miyahara, Bart Devreese, Isabel Vandenberghe, Ayse Hacisalihoglu, Toshihide Okajima, Shun'ichi Kuroda, Osao Adachi, Johannis A Duinel, Jozef Van Beeumen, Katsuyuki Tanizawa, and Ken Hirotsu: "Crystal Structure of Quinohemoprotein Amine Dehydrogenase from Pseudomonas putida"J. Biol. Chem. 277 (4). 2830-2834 (2002)
Description
「研究成果報告書概要(欧文)」より
