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UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
Identifiers
EC no. 1.1.1.335
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
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PMC articles
PubMed articles
NCBI proteins

UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase ( EC 1.1.1.335, WlbA, WbpB) is an enzyme with systematic name UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate:NAD+ 3-oxidoreductase. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction:

UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate + NAD+ UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH + H+

This enzyme participates in the biosynthesis of lipopolysaccharide UDP-alpha-D-ManNAc3NAcA.

References

  1. ^ Westman EL, McNally DJ, Charchoglyan A, Brewer D, Field RA, Lam JS (May 2009). "Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa". The Journal of Biological Chemistry. 284 (18): 11854–62. doi: 10.1074/jbc.M808583200. PMC  2673254. PMID  19282284.
  2. ^ Larkin A, Imperiali B (June 2009). "Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1". Biochemistry. 48 (23): 5446–55. doi: 10.1021/bi900186u. PMC  2694220. PMID  19348502.
  3. ^ Thoden JB, Holden HM (September 2010). "Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid". Biochemistry. 49 (36): 7939–48. doi: 10.1021/bi101103s. PMC  4241754. PMID  20690587.
  4. ^ Thoden JB, Holden HM (March 2011). "Biochemical and structural characterization of WlbA from Bordetella pertussis and Chromobacterium violaceum: enzymes required for the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid". Biochemistry. 50 (9): 1483–91. doi: 10.1021/bi101871f. PMC  3050068. PMID  21241053.

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