PMID:8747459
| Citation |
Oliva, G, Fontes, MR, Garratt, RC, Altamirano, MM, Calcagno, ML and Horjales, E (1995) Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution. Structure 3:1323-32 |
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| Abstract |
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 aldoseketose 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. |
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| Keywords |
Aldose-Ketose Isomerases; Allosteric Regulation; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Carbohydrate Epimerases/antagonists & inhibitors; Carbohydrate Epimerases/chemistry; Carbohydrate Epimerases/metabolism; Catalysis; Crystallography, X-Ray; Enzyme Inhibitors/pharmacology; Escherichia coli/enzymology; Fructosephosphates/biosynthesis; Glucosamine/analogs & derivatives; Glucosamine/metabolism; Glucose-6-Phosphate/analogs & derivatives; Glucosephosphates/metabolism; Macromolecular Substances; Models, Molecular; NAD/metabolism; Phosphates/metabolism; Protein Conformation; Sorbitol/analogs & derivatives; Sorbitol/chemistry; Sorbitol/pharmacology; Sugar Phosphates/chemistry; Sugar Phosphates/pharmacology |
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