UDP-N-acetylglucosamine kinase

UDP-N-acetylglucosamine kinase
Identifiers
EC no.2.7.1.176
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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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 RL, Meinhart A (March 2011). "A novel mechanism of programmed cell death in bacteria by toxin-antitoxin systems corrupts peptidoglycan synthesis". PLOS Biology. 9 (3): e1001033. doi:10.1371/journal.pbio.1001033. PMC 3062530. PMID 21445328.
  2. ^ Rocker A, Meinhart A (August 2015). "A cis-acting antitoxin domain within the chromosomal toxin-antitoxin module EzeT of Escherichia coli quenches toxin activity". Molecular Microbiology. 97 (3): 589–604. doi:10.1111/mmi.13051. PMID 25943309.
  3. ^ Zielenkiewicz U, Ceglowski P (September 2005). "The toxin-antitoxin system of the streptococcal plasmid pSM19035". Journal of Bacteriology. 187 (17): 6094–105. doi:10.1128/JB.187.17.6094-6105.2005. PMC 1196172. PMID 16109951.
  4. ^ Khoo SK, Loll B, Chan WT, Shoeman RL, Ngoo L, Yeo CC, Meinhart A (July 2007). "Molecular and structural characterization of the PezAT chromosomal toxin-antitoxin system of the human pathogen Streptococcus pneumoniae". The Journal of Biological Chemistry. 282 (27): 19606–18. doi:10.1074/jbc.m701703200. hdl:11858/00-001M-0000-002C-A8AD-E. PMID 17488720.