Jump to main content
Jump to site search

Issue 2, 1983
Previous Article Next Article

Mechanism of pyridoxal phosphate-dependent enzymatic amino-acid racemization

Abstract

Conversion of L-[α-2H]alanine in H2O and unlabelled L-alanine in 2H2O into D-alanine, under nearly single-turnover conditions, with tyrosine phenol-lyase and with amino-acid racemase from Pseudomonas striata showed significant internal return of the α-hydrogen; the results support a single base mechanism for the racemization reactions catalysed by these two pyridoxal phosphate enzymes but with a third enzyme, alanine racemase from E. coli, the results were inconclusive, showing no detectable α-hydrogen return.

Back to tab navigation

Article information


J. Chem. Soc., Chem. Commun., 1983, 82-83
Article type
Paper

Mechanism of pyridoxal phosphate-dependent enzymatic amino-acid racemization

S. Shen, H. G. Floss, H. Kumagai, H. Yamada, N. E. K. Soda, S. A. Wasserman and C. Walsh, J. Chem. Soc., Chem. Commun., 1983, 82
DOI: 10.1039/C39830000082

Search articles by author

Spotlight

Advertisements