UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase

Class of enzymes
UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
Identifiers
EC no.2.7.8.33
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase (EC 2.7.8.33, UDP-N-acetylglucosamine:undecaprenyl-phosphate GlcNAc-1-phosphate transferase, WecA, WecA transferase, UDP-GIcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase, GlcNAc-P-P-Und synthase, GPT, TagO, UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase, UDP-N-acetyl-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetylglucosaminephosphotransferase) is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetyl-alpha-D-glucosaminephosphotransferase.[1][2][3][4] This enzyme catalyses the following chemical reaction

UDP-N-acetyl-alpha-D-glucosamine + ditrans, octacis-undecaprenyl phosphate {\displaystyle \rightleftharpoons } UMP + N-acetyl-alpha-D-glucosaminyldiphospho-ditrans, octacis-undecaprenol

This enzyme catalyses the synthesis of ditrans, octacis-undecaprenyl-N-acetyl-alpha-D-glucosaminyl diphosphate.

References

  1. ^ Al-Dabbagh B, Mengin-Lecreulx D, Bouhss A (November 2008). "Purification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA". Journal of Bacteriology. 190 (21): 7141–6. doi:10.1128/jb.00676-08. PMC 2580700. PMID 18723618.
  2. ^ Lehrer J, Vigeant KA, Tatar LD, Valvano MA (April 2007). "Functional characterization and membrane topology of Escherichia coli WecA, a sugar-phosphate transferase initiating the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide". Journal of Bacteriology. 189 (7): 2618–28. doi:10.1128/jb.01905-06. PMC 1855806. PMID 17237164.
  3. ^ Rush JS, Rick PD, Waechter CJ (March 1997). "Polyisoprenyl phosphate specificity of UDP-GlcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase from E.coli". Glycobiology. 7 (2): 315–22. doi:10.1093/glycob/7.2.315. PMID 9134438.
  4. ^ Soldo B, Lazarevic V, Karamata D (July 2002). "tagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168". Microbiology. 148 (Pt 7): 2079–87. doi:10.1099/00221287-148-7-2079. PMID 12101296.
  • UDP-N-acetylglucosamine---undecaprenyl-phosphate+N-acetylglucosaminephosphotransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  • v
  • t
  • e
Transferases: phosphorus-containing groups (EC 2.7)
2.7.1-2.7.4:
phosphotransferase/kinase
(PO4)
2.7.1: OH acceptor
2.7.2: COOH acceptor
2.7.3: N acceptor
2.7.4: PO4 acceptor
2.7.6: diphosphotransferase
(P2O7)2.7.7: nucleotidyltransferase
(PO4-nucleoside)
Polymerase
DNA polymerase
DNA-directed DNA polymerase
I/A
γ
θ
ν
T7
Taq
II/B
α
δ
ε
ζ
Pfu
III/C
IV/X
β
λ
μ
TDT
V/Y
η
ι
κ
RNA-directed DNA polymerase
Reverse transcriptase
Telomerase
RNA polymerase
Phosphorolytic
3' to 5' exoribonuclease
Nucleotidyltransferase
Guanylyltransferase
Other
2.7.8: miscellaneous
Phosphatidyltransferases
Glycosyl-1-phosphotransferase
2.7.10-2.7.13: protein kinase
(PO4; protein acceptor)
2.7.10: protein-tyrosine
2.7.11: protein-serine/threonine
  • see serine/threonine-specific protein kinases
2.7.12: protein-dual-specificity
  • see serine/threonine-specific protein kinases
2.7.13: protein-histidine
Portal:
  • icon Biology