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Titolo:
STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA-COLI AT 2.1-ANGSTROM RESOLUTION
Autore:
OLIVA G; FONTES MRM; GARRATT RC; ALTAMIRANO MM; CALCAGNO ML; HORJALES E;
Indirizzi:
UNIV ESTADUAL PAULISTA JULIO MESQUITA FILHO,IB,DEPT FIS & BIOFIS,CP 510 BR-18618000 BOTUCATU SP BRAZIL UNIV SAO PAULO,INST FIS SAO CARLOS BR-13560970 SAO CARLOS BRAZIL UNIV NACL AUTONOMA MEXICO,FAC MED,DEPT BIOQUIM MEXICO CITY 04510 DF MEXICO
Titolo Testata:
Structure
fascicolo: 12, volume: 3, anno: 1995,
pagine: 1323 - 1332
SICI:
0969-2126(1995)3:12<1323:SACMOG>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; GLUCOSAMINE-6-PHOSPHATE DEAMINASE; PROTEIN MODELS; ISOMERASE; PURIFICATION;
Keywords:
ALDOSE-KETOSE ISOMERASE; ALPHA/BETA OPEN STRUCTURE; ALLOSTERIC ENZYME; NAD-BINDING DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
G. Oliva et al., "STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA-COLI AT 2.1-ANGSTROM RESOLUTION", Structure, 3(12), 1995, pp. 1323-1332

Abstract

Background: Glucosamine 6-phosphate deaminase from Escherichia coli is an allosteric hexameric enzyme which catalyzes the reversible conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate and ammonium ion and is activated by N-acetyl-D-glucosamine 6-phosphate, Mechanistically, it belongs to the group of aldose-ketose isomerases, but its reaction also accomplishes a simultaneous amination/deamination. The determination of the structure of this protein provides fundamental knowledge for understanding its mode of action and the nature of allosteric conformational changes that regulate its function. Results: The crystal structure of glucosamine 6-phosphate deaminase with bound phosphate ions is presented at 2.1 Angstrom resolution together with the refined structures of the enzyme in complexes with its allosteric activator and with a competitive inhibitor. The protein fold can be described as a modified NAD-binding domain. Conclusions: From the similarities between the three presented structures, it is concluded that these represent the enzymatically active R state conformer. A mechanism for the deaminase reaction is proposed. It comprises steps to open the pyranose ring of the substrate and a sequence of general base-catalyzed reactions to bring about isomerization and deamination, with Asp72 playing a key role as a proton exchanger.

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Documento generato il 19/09/20 alle ore 12:56:29