| Type: | Conserved_site | Name: | Glucosamine-6-phosphate isomerase, conserved site |
| Description: | Glucosamine-6-phosphate isomerase () catalyses the conversion of D-glucosamine 6-phosphate (GlcN6P) to D-fructose 6-phosphate and ammonia. This is the last step in the pathway for N-acetylglucosamine (GlcNAC) utilization in bacteria such as Escherichia coli(gene nagB) or in fungi such as Candida albicans(Yeast) (gene NAG1). The structure of this enzyme from E. coli (NagB) is described as a modified NAD-binding domain, and undergoes allosteric conformational changes that regulate its function []. The reaction steps involve opening of the pyranose ring of the substrate and a sequence of general base-catalysed reactions to bring about isomerisation and deamination [].This entry represents a conserved region located in the central part of these enzymes. This region contains a conserved histidine which has been shown [], in NagB, to be important for the pyranose ring-opening step of the catalytic mechanism. | Short Name: | Glucosamine6P_isomerase_CS |
