Issue 2, 1993

Stereospecific lysis of a range of β-hydroxy-α-amino acids catalysed by a novel aldolase from Streptomyces amakusaensis

Abstract

Cell-free preparations of Streptomyces amakusaensis contain a novel aldolase which catalyses the conversion of β-hydroxy-α-amino acids (as 2) into the corresponding aldehyde plus glycine; the aldolase is stable, shows broad substrate tolerance, is highly selective for threo stereochemistry and, where examined, is Stereospecific for the (2S,3R) configuration.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1993, 205-206

Stereospecific lysis of a range of β-hydroxy-α-amino acids catalysed by a novel aldolase from Streptomyces amakusaensis

R. B. Herbert, B. Wilkinson, G. J. Ellames and E. K. Kunec, J. Chem. Soc., Chem. Commun., 1993, 205 DOI: 10.1039/C39930000205

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