The critical structural role of a highly conserved histidine residue in group II amino acid decarboxylases

  • Capitani G
  • Tramonti A
  • Bossa F
 et al. 
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Abstract

Glutamate decarboxylase is a pyridoxal 5′-phosphate (PLP)-dependent enzyme, belonging to the subset of PLP-dependent decarboxylases classified as group II. Site-directed mutagenesis of Escherichia coli glutamate decarboxylase, combined with analysis of the crystal structure, shows that a histidine residue buried in the protein core is critical for correct folding. This histidine is strictly conserved in the PF00282 PFAM family, which includes the group II decarboxylases. A similar role is proposed for residue Ser269, also highly conserved in this group of enzymes, as it provides one of the interactions stabilising His241. © 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Author-supplied keywords

  • Glutamate decarboxylase
  • Histidine residue
  • Pyridoxal 5′-phosphate
  • Stabilising interaction

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