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Titolo:
Contribution of an aspartate residue, D114, in the active site of clostridial glutamate dehydrogenase to the enzyme's unusual pH dependence
Autore:
Coughlan, S; Wang, XG; Britton, KL; Stillman, TJ; Rice, DW; Chiaraluce, R; Consalvi, V; Scandurra, R; Engel, PC;
Indirizzi:
Natl Univ Ireland Univ Coll Dublin, Dept Biochem, Dublin 4, Ireland Natl Univ Ireland Univ Coll Dublin Dublin Ireland 4 m, Dublin 4, Ireland Natl Univ Ireland Univ Coll Dublin, Conway Inst Biomol & Biomed Res, Dublin 4, Ireland Natl Univ Ireland Univ Coll Dublin Dublin Ireland 4 s, Dublin 4, Ireland Univ Sheffield, Dept Mol Biol & Biotechnol, Krebs Inst Biomol Res, Sheffield S10 2UH, S Yorkshire, England Univ Sheffield Sheffield S Yorkshire England S10 2UH S Yorkshire, England Univ La Sapienza, Dipartimento Sci Biochim, I-00185 Rome, Italy Univ La Sapienza Rome Italy I-00185 nto Sci Biochim, I-00185 Rome, Italy
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
fascicolo: 1-2, volume: 1544, anno: 2001,
pagine: 10 - 17
SICI:
0167-4838(20010112)1544:1-2<10:COAARD>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANAEROBIC-BACTERIA; ESCHERICHIA-COLI; SYMBIOSUM; MUTAGENESIS;
Keywords:
glutamate dehydrogenase; mutagenesis; pH dependence; structural comparison;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Engel, PC Natl Univ Ireland Univ Coll Dublin, Dept Biochem, Dublin 4, Ireland Natl Univ Ireland Univ Coll Dublin Dublin Ireland 4 4, Ireland
Citazione:
S. Coughlan et al., "Contribution of an aspartate residue, D114, in the active site of clostridial glutamate dehydrogenase to the enzyme's unusual pH dependence", BBA-PROT ST, 1544(1-2), 2001, pp. 10-17

Abstract

Glutamate dehydrogenase from Clostridium symbiosum displays unusual kinetic behaviour at high pH when compared with other members of this enzyme family. Structural and sequence comparisons with GDHs from other organisms haveindicated that the Asp residue at position 114 in the clostridial enzyme may account for these differences. By replacing this residue by Asn, a mutant protein has been created with altered functional properties at high pH, This mutant protein can be efficiently overexpressed in Escherichia coli, and several criteria, including mobility in non-denaturing electrophoresis, circular dichroism (CD) spectra and initial crystallisation studies, suggesta folding and an assembly comparable to those of the wild-type protein. The D114N mutant enzyme shows a higher optimum pH for activity than the wild-type enzyme, and both CD data and activity measurements show that the distinctive time-dependent reversible conformational inactivation seen at high pH in the wild-type enzyme is abolished in the mutant. (C) 2001 Elsevier Science B.V. All rights reserved.

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Documento generato il 10/07/20 alle ore 12:45:49