The Enzyme Database

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EC 2.3.1.157     
Accepted name: glucosamine-1-phosphate N-acetyltransferase
Reaction: acetyl-CoA + α-D-glucosamine 1-phosphate = CoA + N-acetyl-α-D-glucosamine 1-phosphate
For diagram of the biosynthesis of UDP-N-acetylglucosamine, click here
Systematic name: acetyl-CoA:α-D-glucosamine-1-phosphate N-acetyltransferase
Comments: The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Hemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-91-8
References:
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]
[EC 2.3.1.157 created 2001]
 
 


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