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2003 Fiscal Year Final Research Report Summary

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)
Project Period (FY) 2002 – 2003
KeywordsD-amino acid / racemase / eukaryote / yeast / D-amino acid N-acetyltransferase
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.

  • Research Products

    (4 results)

All Other

All Publications (4 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
  • [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
  • [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
  • [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

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Published: 2005-04-19  

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