UDP-N-acetylglucosamine kinase

UDP-N-acetylglucosamine kinase
Identifiers
EC number 2.7.1.176
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

UDP-N-acetylglucosamine kinase (EC 2.7.1.176, UNAG kinase, zeta toxin, toxin PezT, ATP:UDP-N-acetyl-D-glucosamine 3'-phosphotransferase) is an enzyme with systematic name ATP:UDP-N-acetyl-alpha-D-glucosamine 3'-phosphotransferase.[1][2] This enzyme catalyses the following chemical reaction

ATP + UDP-N-acetyl-alpha-D-glucosamine ADP + UDP-N-acetyl-alpha-D-glucosamine 3'-phosphate

The phosphorylation of UDP-N-acetyl-D-glucosamine causes the inhibition of enzyme EC 2.5.1.7, UDP-N-acetylglucosamine 1-carboxyvinyltransferase.

These enzymes are found as part of plasmid-encoded[3] and chromosomal[4] bacterial toxin-antitoxin systems.

References

  1. Mutschler, H.; Gebhardt, M.; Shoeman, R.L.; Meinhart, A. (2011). "A novel mechanism of programmed cell death in bacteria by toxin-antitoxin systems corrupts peptidoglycan synthesis". PLoS Biol. 9: #e1001033–e1001033. doi:10.1371/journal.pbio.1001033. PMC 3062530Freely accessible. PMID 21445328.
  2. Rocker, A.; Meinhart, A. (2015). "A cis-acting antitoxin domain within the chromosomal toxin-antitoxin module EzeT of Escherichia coli quenches toxin activity". Mol Microbiol. 97: 589–604. doi:10.1111/mmi.13051. PMID 25943309.
  3. Zielenkiewicz U.; Cegłowski P. (2005). "The Toxin-Antitoxin System of the Streptococcal Plasmid pSM19035". J Bacteriol. 187: 6094–6105. doi:10.1128/JB.187.17.6094-6105.2005. PMID 16109951.
  4. Khoo, S.K.; Loll, B.; Chan, W.T.; Shoeman, R.L.; Ngoo, L.; Yeo, C.C.; Meinhart, A. (2007). "Molecular and structural characterization of the PezAT chromosomal toxin-antitoxin system of the human pathogen Streptococcus pneumoniae". J. Biol. Chem. 282: 19606–19618. doi:10.1074/jbc.m701703200. PMID 17488720.
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