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.
CITATION STYLE
Capitani, G., Tramonti, A., Bossa, F., Grütter, M. G., & De Biase, D. (2003). The critical structural role of a highly conserved histidine residue in group II amino acid decarboxylases. FEBS Letters, 554(1–2), 41–44. https://doi.org/10.1016/S0014-5793(03)01079-2
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