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

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Short description: Class of enzymes
UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
Identifiers
EC number2.7.8.33
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 [math]\displaystyle{ \rightleftharpoons }[/math] 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. "Purification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA". Journal of Bacteriology 190 (21): 7141–6. November 2008. doi:10.1128/jb.00676-08. PMID 18723618. 
  2. "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. April 2007. doi:10.1128/jb.01905-06. PMID 17237164. 
  3. "Polyisoprenyl phosphate specificity of UDP-GlcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase from E.coli". Glycobiology 7 (2): 315–22. March 1997. doi:10.1093/glycob/7.2.315. PMID 9134438. 
  4. "tagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168". Microbiology 148 (Pt 7): 2079–87. July 2002. doi:10.1099/00221287-148-7-2079. PMID 12101296. 

External links