| 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 |
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For diagram of UDP-N-acetylglucosamine biosynthesis, 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 Haemophilus 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 11329257] |
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| [EC 2.3.1.157 created 2001] |
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