Glucosamine-6-phosphate deaminase

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glucosamine-6-phosphate deaminase
Identifiers
EC number 3.5.99.6
CAS number 9013-10-9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

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 glucosamine 6-phosphate and H2O, whereas its two products are 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.

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.

References

    • COMB DG, ROSEMAN S (1958). "Glucosamine metabolism. IV. Glucosamine-6-phosphate deaminase". J. Biol. Chem. 232 (2): 80727. PMID 13549465. 
    • Pattabiraman TN, Bachhawat BK (1961). "Purification of glucosamine 6-phosphate deaminase from human brain". Biochim. Biophys. Acta 54 (2): 273283. doi:10.1016/0006-3002(61)90366-3. PMID 14484386. 
    • Wolfe JB, Britton BB, Nakada HI (1957). "Glucosamine degradation by Escherichia coli. III. Isolation and studies of "phosphoglucosaminisomerase"". Arch. Biochem Biophys. 66 (2): 333339. doi:10.1016/S0003-9861(57)80008-3. 


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