EC |
2.7.1.176 |
Accepted name: |
UDP-N-acetylglucosamine kinase |
Reaction: |
ATP + UDP-N-acetyl-α-D-glucosamine = ADP + UDP-N-acetyl-α-D-glucosamine 3′-phosphate |
Other name(s): |
UNAG kinase; ζ toxin; toxin PezT; ATP:UDP-N-acetyl-D-glucosamine 3′-phosphotransferase |
Systematic name: |
ATP:UDP-N-acetyl-α-D-glucosamine 3′-phosphotransferase |
Comments: |
Toxic component of a toxin-antitoxin (TA) module. The phosphorylation of UDP-N-acetyl-D-glucosamine results in the inhibition of EC 2.5.1.7, UDP-N-acetylglucosamine 1-carboxyvinyltransferase, the first committed step in cell wall synthesis, which is then blocked. The activity of this enzyme is inhibited when the enzyme binds to the cognate ε antitoxin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Khoo, S.K., Loll, B., Chan, W.T., Shoeman, R.L., Ngoo, L., Yeo, C.C. and Meinhart, A. Molecular and structural characterization of the PezAT chromosomal toxin-antitoxin system of the human pathogen Streptococcus pneumoniae. J. Biol. Chem. 282 (2007) 19606–19618. [DOI] [PMID: 17488720] |
2. |
Mutschler, H., Gebhardt, M., Shoeman, R.L. and Meinhart, A. A novel mechanism of programmed cell death in bacteria by toxin-antitoxin systems corrupts peptidoglycan synthesis. PLoS Biol. 9:e1001033 (2011). [DOI] [PMID: 21445328] |
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[EC 2.7.1.176 created 2012] |
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