PMID:10378272
| Citation |
Horjales, E, Altamirano, MM, Calcagno, ML, Garratt, RC and Oliva, G (1999) The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution. Structure 7:527-37 |
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| Abstract |
The allosteric hexameric enzyme glucosamine-6-phosphate deaminase from Escherichia coli catalyses the regulatory step of N-acetylglucosamine catabolism, which consists of the isomerisation and deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonia. The reversibility of the catalysis and its rapid-equilibrium random kinetic mechanism, among other properties, make this enzyme a good model for studying allosteric processes. |
| Links | |
| Keywords |
Aldose-Ketose Isomerases/chemistry; Allosteric Regulation; Binding Sites; Catalysis; Escherichia coli/enzymology; Fructosephosphates/metabolism; Glucosamine/analogs & derivatives; Glucosamine/metabolism; Glucose-6-Phosphate/analogs & derivatives; Glucose-6-Phosphate/metabolism; Kinetics; Protein Conformation; Static Electricity |
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