Issue 2, 1983

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.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1983, 82-83

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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements