UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase explained
| UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase |
| Ec Number: | 1.1.1.335 |
UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase (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.
Notes and References
- Westman EL, McNally DJ, Charchoglyan A, Brewer D, Field RA, Lam JS . 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 . May 2009 . 19282284 . 2673254 . 10.1074/jbc.M808583200 . free .
- Larkin A, Imperiali B . 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 . June 2009 . 19348502 . 2694220 . 10.1021/bi900186u .
- Thoden JB, Holden HM . 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 . September 2010 . 20690587 . 4241754 . 10.1021/bi101103s .
- Thoden JB, Holden HM . 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 . March 2011 . 21241053 . 3050068 . 10.1021/bi101871f .
