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

This is an abbreviated version!
For detailed information about UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.335

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+

Synonyms

PGN_0168, WblA, WbpB, WlbA

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.335 UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase

Systematic Name

Systematic Name on EC 1.1.1.335 - UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase

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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate:NAD+ 3-oxidoreductase
This enzyme participates in the biosynthetic pathway for UDP-alpha-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalysing the next step the pathway (EC 2.6.1.98, UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase). The enzyme also possesses an EC 1.1.99.2 (L-2-hydroxyglutarate dehydrogenase) activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD+. The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD+ as tightly and do not require 2-oxoglutarate to function.