Reaction: acetyl-CoA + α-D-glucosamine 1-phosphate = CoA + N-acetyl-α-D-glucosamine 1-phosphate
For diagram click here.
Other Name(s): acetyl-CoA:D-glucosamine-1-phosphate N-acetyltransferase
Systematic name: acetyl-CoA:α-D-glucosamine-1-phosphate N-acetyltransferase
Comments: The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 18.104.22.168, UDP-N-acetylglucosamine diphosphorylase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-91-8
1. Mengin-Lecreulx, D. and van Heijenoort, J. 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: (1994) 5788-5795. [PMID: 8083170]
2. Gehring, A.M., Lees, W.J., Mindiola, D.J., Walsh, C.T. and Brown, E.D. Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli. Biochemistry 35 (1996) 579-585. [PMID: 8555230]
3. Olsen, L.R. and Roderick, S.L. Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites. Biochemistry 40 (2001) 1913-1921. [PMID: 11329257]