Stereochemistry of the hydrogen abstraction from pyridoxamine phosphate catalyzed by alanine racemase of Bacillus stearothermophilus

Akira Watanabe, Tohru Yoshimura, Young Hee Lim, Yoichi Kurokawa, Kenji Soda, Nobuyoshi Esaki

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

Alanine racemase of Bacillus stearothermophilus catalyzes transamination as a side reaction. Stereospecificity for the hydrogen abstraction from C-4′ of pyridoxamine 5′-phosphate occurring in the latter half transamination was examined. Both apo-wild-type and apo-fragmentary alanine racemases abstracted approximately 20 and 80% of tritium from the stereospecifically-labeled (4′S)- and (4′R)-[4′-3H]PMP, respectively, in the presence of pyruvate. Alanine racemase catalyzes the abstraction of both 4′S- and 4′R-hydrogen like amino acid racemase with broad substrate specificity. However, R-isomer preference is a characteristic property of alanine racemase.

Original languageEnglish
Pages (from-to)145-150
Number of pages6
JournalJournal of Molecular Catalysis - B Enzymatic
Volume12
Issue number1-6
DOIs
Publication statusPublished - 2001 Feb 28
Externally publishedYes

Keywords

  • Alanine racemase
  • Pyridoxal 5′-phosphate
  • Stereochemistry
  • Transamination

ASJC Scopus subject areas

  • Catalysis
  • Bioengineering
  • Biochemistry
  • Process Chemistry and Technology

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