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
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1.1.1.335
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retroviral
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capsid
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retroviruses
-
trim5alpha
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rhesus
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tripartite
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cyclophilin
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antiretroviral
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simian
-
macaque
-
trimcyps
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anti-hiv-1
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trim5-cyclophilin
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indian-origin
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post-entry
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sivmac239
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trim22
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spry
-
alpha-mediated
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synthesis
- 1.1.1.335
-
retroviral
-
capsid
-
retroviruses
- trim5alpha
-
rhesus
-
tripartite
- cyclophilin
-
antiretroviral
-
simian
-
macaque
-
trimcyps
-
anti-hiv-1
-
trim5-cyclophilin
-
indian-origin
-
post-entry
-
sivmac239
- trim22
-
spry
-
alpha-mediated
- synthesis
Reaction
Synonyms
PGN_0168, WblA, WbpB, WlbA
ECTree
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Systematic Name
Systematic Name on EC 1.1.1.335 - UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
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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.