Biology:Glucosamine-1-phosphate N-acetyltransferase
From HandWiki
glucosamine-1-phosphate N-acetyltransferase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 2.3.1.157 | ||||||||
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 / QuickGO | ||||||||
|
In enzymology, a glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157) is an enzyme that catalyzes the chemical reaction
- acetyl-CoA + alpha-D-glucosamine 1-phosphate [math]\displaystyle{ \rightleftharpoons }[/math] CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
Thus, the two substrates of this enzyme are acetyl-CoA and alpha-D-glucosamine 1-phosphate, whereas its two products are CoA and N-acetyl-alpha-D-glucosamine 1-phosphate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:alpha-D-glucosamine-1-phosphate N-acetyltransferase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2OI5, 2OI6, and 2OI7.
References
- "Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis". J. Bacteriol. 176 (18): 5788–95. 1994. doi:10.1128/jb.176.18.5788-5795.1994. PMID 8083170.
Original source: https://en.wikipedia.org/wiki/Glucosamine-1-phosphate N-acetyltransferase.
Read more |