From Wikipedia, the free encyclopedia
GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase
Identifiers
EC no. 2.4.1.292
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

GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase ( EC 2.4.1.292, PglH) is an enzyme with systematic name UDP-N-acetyl-alpha-D-galactosamine:GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-tritrans,heptacis-undecaprenol 4-alpha-N-acetyl-D-galactosaminyltransferase. [1] [2] [3] This enzyme catalyses the following chemical reaction

3 UDP-N-acetyl-alpha-D-galactosamine + GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-tritrans,heptacis-undecaprenol 3 UDP + [GalNAc-alpha-(1->4)]4-GalNAc-alpha-(1->3)-diNAcBac-PP-tritrans,heptacis-undecaprenol

This enzyme is solated from Campylobacter jejuni.

References

  1. ^ Glover KJ, Weerapana E, Imperiali B (October 2005). "In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation". Proceedings of the National Academy of Sciences of the United States of America. 102 (40): 14255–9. Bibcode: 2005PNAS..10214255G. doi: 10.1073/pnas.0507311102. PMC  1242339. PMID  16186480.
  2. ^ Troutman JM, Imperiali B (March 2009). "Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions". Biochemistry. 48 (12): 2807–16. doi: 10.1021/bi802284d. PMC  2736683. PMID  19159314.
  3. ^ Børud B, Viburiene R, Hartley MD, Paulsen BS, Egge-Jacobsen W, Imperiali B, Koomey M (June 2011). "Genetic and molecular analyses reveal an evolutionary trajectory for glycan synthesis in a bacterial protein glycosylation system". Proceedings of the National Academy of Sciences of the United States of America. 108 (23): 9643–8. Bibcode: 2011PNAS..108.9643B. doi: 10.1073/pnas.1103321108. PMC  3111294. PMID  21606362.

External links

From Wikipedia, the free encyclopedia
GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase
Identifiers
EC no. 2.4.1.292
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

GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase ( EC 2.4.1.292, PglH) is an enzyme with systematic name UDP-N-acetyl-alpha-D-galactosamine:GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-tritrans,heptacis-undecaprenol 4-alpha-N-acetyl-D-galactosaminyltransferase. [1] [2] [3] This enzyme catalyses the following chemical reaction

3 UDP-N-acetyl-alpha-D-galactosamine + GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-tritrans,heptacis-undecaprenol 3 UDP + [GalNAc-alpha-(1->4)]4-GalNAc-alpha-(1->3)-diNAcBac-PP-tritrans,heptacis-undecaprenol

This enzyme is solated from Campylobacter jejuni.

References

  1. ^ Glover KJ, Weerapana E, Imperiali B (October 2005). "In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation". Proceedings of the National Academy of Sciences of the United States of America. 102 (40): 14255–9. Bibcode: 2005PNAS..10214255G. doi: 10.1073/pnas.0507311102. PMC  1242339. PMID  16186480.
  2. ^ Troutman JM, Imperiali B (March 2009). "Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions". Biochemistry. 48 (12): 2807–16. doi: 10.1021/bi802284d. PMC  2736683. PMID  19159314.
  3. ^ Børud B, Viburiene R, Hartley MD, Paulsen BS, Egge-Jacobsen W, Imperiali B, Koomey M (June 2011). "Genetic and molecular analyses reveal an evolutionary trajectory for glycan synthesis in a bacterial protein glycosylation system". Proceedings of the National Academy of Sciences of the United States of America. 108 (23): 9643–8. Bibcode: 2011PNAS..108.9643B. doi: 10.1073/pnas.1103321108. PMC  3111294. PMID  21606362.

External links


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