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Updated: Jun 13, 2026

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
Published on: October 13, 2022
Molecular modeling studies of the conserved B(12)-binding motif and its variants from Clostridium tetanomorphum
1Department of Agricultural Chemistry, National Taiwan University, Taipei, Taiwan. andyhsu@ntu.edu.tw
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 B(12)-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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