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. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
The critical structural role of a highly conserved histidine residue in group II amino acid decarboxylases / Guido, Capitani; Angela, Tramonti; Bossa, Francesco; Markus G., Grutter; DE BIASE, Daniela. - In: FEBS LETTERS. - ISSN 0014-5793. - STAMPA. - 554:1-2(2003), pp. 41-44. [10.1016/s0014-5793(03)01079-2]
The critical structural role of a highly conserved histidine residue in group II amino acid decarboxylases
BOSSA, Francesco;DE BIASE, Daniela
2003
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. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
