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

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UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
Identifiers
EC no.1.1.1.335
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
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NCBIproteins

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

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  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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