From Wikipedia, the free encyclopedia
UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
Identifiers
EC no. 2.7.8.33
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

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 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.

External links

From Wikipedia, the free encyclopedia
UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
Identifiers
EC no. 2.7.8.33
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

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 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.

External links


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