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

Chun-Hua      Hsu; Hao-Ping      Chen

doi:10.2174/092986610791190264

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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Protein & Peptide Letters

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

Volume: 17 Issue: 6

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

Affiliation:

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

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.

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Hsu Chun-Hua and Chen Hao-Ping, Molecular Modeling Studies of the Conserved B12-Binding Motif and Its Variants from Clostridium tetanomorphum Glutamate Mutase, Protein & Peptide Letters 2010; 17 (6) . https://dx.doi.org/10.2174/092986610791190264

DOI https://dx.doi.org/10.2174/092986610791190264	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305

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