Issue 18, 2011

Structural and biochemical analyses reveal how ornithineacetyl transferase binds acidic and basic amino acid substrates

Abstract

Structural and biochemical analyses reveal how ornithine acetyl-transferases catalyse the reversible transfer of an acetyl-group from a basic (ornithine) to an acidic (glutamate) amino acid by employing a common mechanism involving an acetyl-enzyme intermediate but using different side chain binding modes.

Graphical abstract: Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates

Supplementary files

Article information

Article type
Paper
Submitted
07 Apr 2011
Accepted
25 May 2011
First published
28 Jul 2011

Org. Biomol. Chem., 2011,9, 6219-6225

Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates

A. Iqbal, Ian. J. Clifton, R. Chowdhury, D. Ivison, C. Domene and C. J. Schofield, Org. Biomol. Chem., 2011, 9, 6219 DOI: 10.1039/C1OB05554B

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.

Social activity

Spotlight

Advertisements