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

FEBS Letters

Bossa, Francesco¹  Grütter, Markus G.²  Capitani, Guido²  Tramonti, Angela³  De Biase, Daniela¹ 

[1] Dipartimento di Scienze Biochimiche ‘A. Rossi Fanelli’, Università La Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy;Biochemisches Institut der Universität Zürich, Winterthurerstrasse 190, 8057 Zürich Switzerland;Istituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Università La Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy

关键词: Glutamate decarboxylase;    Histidine residue;    Pyridoxal 5′-phosphate;    Stabilising interaction;    Gad;    glutamate decarboxylase;    PLP;    pyridoxal 5′-phosphate;   

DOI  :  10.1016/S0014-5793(03)01079-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown