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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Molecular Modeling Studies of the Conserved B12-Binding Motif and Its Variants from Clostridium tetanomorphum Glutamate Mutase

Author(s): Chun-Hua Hsu and Hao-Ping Chen

Volume 17, Issue 6, 2010

Page: [759 - 764] Pages: 6

DOI: 10.2174/092986610791190264

Price: $65

Abstract

The coupling of an aspartate residue with an active site histidine plays a pivotal role in enzyme catalysis. The His-Asp pair in glutamate mutase and other B12-dependent mutases is not only responsible for coenzyme-binding, but is also involved in fine-tuning the enzymatic activities. Our modeling results show that the His-Asp pair is arranged in a highly organized manner. Except for carboxymethylated Cys or Glu, a less hindered or non-charged amino acid residue is preferred between the conserved histidine and aspartate residue.

Keywords: Glutamate mutase, B12, cobalamin, adenosylcobalamin, modeling


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