Glucosamine-6-phosphate deaminase

From Wikipedia, the free encyclopedia

In enzymology, a glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an enzyme that catalyzes the chemical reaction

D-glucosamine 6-phosphate + H2O \rightleftharpoons D-fructose 6-phosphate + NH3

Thus, the two substrates of this enzyme are D-glucosamine 6-phosphate and H2O, whereas its two products are D-fructose 6-phosphate and NH3.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing). Other names in common use include glucosaminephosphate isomerase, glucosamine-6-phosphate isomerase, phosphoglucosaminisomerase, glucosamine phosphate deaminase, aminodeoxyglucosephosphate isomerase, and phosphoglucosamine isomerase. This enzyme participates in aminosugars metabolism. This enzyme has at least one effector, N-Acetyl-D-glucosamine 6-phosphate.

Contents

[edit] Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1J5X, 1JT9, 1NE7, 2BKV, and 2BKX.

[edit] References

[edit] External links

The CAS registry number for this enzyme class is 9013-10-9.

[edit] Gene Ontology (GO) codes

 This hydrolase article is a stub. You can help Wikipedia by expanding it.