EC 1 - Oxidoreductases
EC 1.1 - Acting on the CH-OH group of donors
EC 1.1.1 - With NAD+ or NADP+ as acceptor
EC 1.1.1.305 - UDP-glucuronic acid oxidase (UDP-4-keto-hexauronic acid decarboxylating)
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.1.1.305
Names
Accepted name:
UDP-glucuronic acid oxidase (UDP-4-keto-hexauronic acid decarboxylating)
Other
names:
UDP-GlcUA decarboxylase
ArnADH
UDP-glucuronate:NAD+ oxidoreductase (decarboxylating)
ArnADH
UDP-glucuronate:NAD+ oxidoreductase (decarboxylating)
Systematic name:
UDP-α-D-glucuronate:NAD+ oxidoreductase (decarboxylating)
Reaction
- UDP-alpha-D-glucuronate + NAD+ = UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
Comments:
The activity is part of a bifunctional enzyme also performing the reaction of EC 2.1.2.13 (UDP-4-amino-4-deoxy-L-arabinose formyltransferase).
Links to other databases
Gene Ontology:
GO:0099618
References
-
A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose. Identification and function of UDP-4-deoxy-4-formamido-L-arabinose.J. Biol. Chem. 280 : 14154-14167 (2005). [PMID: 15695810]
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Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance.Biochemistry 43 : 13370-13379 (2004). [PMID: 15491143]
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Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis.J. Biol. Chem. 280 : 23000-23008 (2005). [PMID: 15809294]
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Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance.Structure 13 : 929-942 (2005). [PMID: 15939024]
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An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli.J. Biol. Chem. 282 : 36077-36089 (2007). [PMID: 17928292]
[EC 1.1.1.305 created 2010]