• Search Research Projects
  • Search Researchers
  • How to Use
  1. Back to previous page

Studies of physiological function of D-aspartate in eukaryotic cells : from yeasts to mammals

Research Project

Project/Area Number 14560064
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field 応用微生物学・応用生物化学
Research InstitutionNagoya University (2003)
Kyoto University (2002)

Principal Investigator

MORIYAMA Ryuichi  Nagoya University, Graduate School of Bioagricultural Science, Associate Professor, 大学院・生命農学研究科, 教授 (70182821)

Co-Investigator(Kenkyū-buntansha) 森山 龍一  名古屋大学, 大学院・生命農学研究科, 助教授 (60191061)
三原 久明  京都大学, 化学研究所, 助手 (30324693)
栗原 達夫  京都大学, 化学研究所, 助手 (70243087)
江崎 信芳  京都大学, 化学研究所, 教授 (50135597)
Project Period (FY) 2002 – 2003
Project Status Completed (Fiscal Year 2003)
Budget Amount *help
¥4,100,000 (Direct Cost: ¥4,100,000)
Fiscal Year 2003: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 2002: ¥2,500,000 (Direct Cost: ¥2,500,000)
KeywordsD-amino acid / racemase / eukaryote / yeast / D-amino acid N-acetyltransferase / N-アセチル-D-アミノ酸 / D-アミノ酸 N-アセチルトランスフェラーゼ / 分裂酵母
Research Abstract

We studied functions of the eukaryotic genes encoding putative D-amino acid-related enzymes. We found that dao 1^+, alr 1^+, alr 2^+, and srf1^+ of Schizosaccharomyces pombe encode D-amino acid oxidase, alanine racemase, arginine racemase, and serine racemase, respectively. Saccharomyces cerevisiae cells were reported to contain D-amino acid N-acetyltransferase, however its gene has been unknown. We found that the enzyme is encoded by HPA3, the gene of a putative histone/protein acetyltransferase belonging to Gcn5-related N-acetyltransferase superfamily. The gene product, Hpa3p, acts on a wide range of D-amino acids but none of L-amino acids. Hpa3p shares 49% sequence identity and 81% sequence similarity with Hpa2p, a yeast histone acetyltransferase. However, Hpa3p shows little histone acetyltransferase activity, and Hpa2p has no detectable acetyltransferase activities towards D-or L-amino acids tested except for the trace activity towards D-and L-lysine. Kinetic analyses suggest that Hpa3p catalyzes the acetylation of D-amino acids with an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to leave. Hpa3p was revealed to be involved in lowering the inhibitoru effect of various D-amino acids. We also studied the function of the mouse PROSC protein, a homolog of S. cerevisiae Yb1036cp, which has no sequencial homology but has similar three-dimensional structure to that of the N-terminal domain of bacterial alanine racemase.

Report

(3 results)
  • 2003 Annual Research Report   Final Research Report Summary
  • 2002 Annual Research Report
  • Research Products

    (8 results)

All Other

All Publications (8 results)

  • [Publications] Yow G.-Y., Watanabe, A., Yoshimura, T., Esaki, N.: "Conversion of the catalytic specificity of alanine racemase to a D-amino acid aminotransferase activity by a double active-site mutation"Journal of Molecular Catalysis B : Enzymatic. 23. 311-319 (2003)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2003 Final Research Report Summary
  • [Publications] Fuchikami Y, Yoshimura, T., Esaki, N.: "D-Amino acid aminotransferase : fragmentation at a flexible loop is an efficient method to generate mutant enzymes with new substrate specificities and elevated activities."Journal of Molecular Catalysis B : Enzymatic. 23. 321-328 (2003)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2003 Final Research Report Summary
  • [Publications] Yow G.-Y., Watanabe, A., Yoshimura, T., Esaki, N.: "Conversion of the catalytic specificity of alanine racemase to a D-amino acid aminotransferase activity by a double active-site mutation"Journal of Molecular Catalysis B : Enzymatic. 23. 311-319 (2003)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2003 Final Research Report Summary
  • [Publications] Fuchikami Y., Yoshimura, T., Esaki, N.: "D-Amino acid aminotransferase : fragmentation at a flexible loop is an efficient method to generate mutant enzymes with new substrate specificities arid elevated activities."Journal of Molecular Catalysis B : Enzymatic. 23. 321-328 (2003)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2003 Final Research Report Summary
  • [Publications] Yow G.-Y., Watanabe A., Yoshimura T., Esaki, N.: "Conversion of the catalytic specificity of alanine racemase to a D-amino acid aminotransferase activity by a double active-site mutation"Journal of Molecular Catalysis B : Enzymatic. 23. 311-319 (2003)

    • Related Report
      2003 Annual Research Report
  • [Publications] Fuchikami Y., Yoshimura, T., Esaki, N.: "D-Amino acid aminotransferase : fragmentation at a flexible loop is an efficient method to generate mutant enzymes with new substrate specificities and elevated activities"Journal of Molecular Catalysis B : Enzymatic. 23. 321-328 (2003)

    • Related Report
      2003 Annual Research Report
  • [Publications] Watanabe, A.: "Reaction mechanism of alanine racemase from Bacillus stearothermophilus : X-ray crystallographic studies of the enzyme bound with N-(5'-phosphopyridoxyl)-alanine"J. Biol. Chem.. 277. 19166-19172 (2002)

    • Related Report
      2002 Annual Research Report
  • [Publications] Uo, T.: "Gene coning, purification, and characterization of 2,3-diaminopropionate ammonia-lyase from Escherichia coli"Biosci. Biotechnol. Biochem.. 66. 2639-2644 (2002)

    • Related Report
      2002 Annual Research Report

URL: 

Published: 2002-04-01   Modified: 2016-04-21  

Information User Guide FAQ News Terms of Use Attribution of KAKENHI

Powered by NII kakenhi