Issue 48, 2006
From the journal:

Chemical Communications

Mechanism and substrate stereochemistry of 2-amino-3-oxobutyrate CoA ligase: implications for 5-aminolevulinate synthase and related enzymes†

Qamar Bashir,a   Naeem Rashida  and  Muhammad Akhtar*ab  

* Corresponding authors

a School of Biological Sciences, University of the Punjab, New Campus, Lahore, Pakistan
E-mail: sobs@cyber.net.pk
Fax: +92 42 9230980
Tel: +92 42 9230960

b School of Biological Sciences, University of Southampton, Southampton, UK
E-mail: ma3@soton.ac.uk
Fax: +44 23 80594459
Tel: +44 23 80594338

Abstract

The condensation process catalysed by 2-amino-3-oxobutyrate CoA ligase (KBL; also known as 2-amino-3-ketobutyrate ligase) involves the loss of the pro-R hydrogen atom of glycine and occurs with the inversion of stereochemistry; a similar scenario is envisaged for the condensation step of other α-oxoamine synthases.

Graphical abstract: Mechanism and substrate stereochemistry of 2-amino-3-oxobutyrate CoA ligase: implications for 5-aminolevulinate synthase and related enzymes

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Article information

DOI
https://doi.org/10.1039/B609925D
Article type
Communication
Submitted
12 Jul 2006
Accepted
20 Sep 2006
First published
13 Oct 2006

Chem. Commun., 2006, 5065-5067

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Mechanism and substrate stereochemistry of 2-amino-3-oxobutyrate CoA ligase: implications for 5-aminolevulinate synthase and related enzymes

Q. Bashir, N. Rashid and M. Akhtar, Chem. Commun., 2006, 5065 DOI: 10.1039/B609925D

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