UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase

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+
UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
Identifiers
EC number1.1.1.335
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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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