ExplorEnz: EC 1.1.1.305

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1.1.1.305

Accepted name:

UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)

Reaction:

UDP-α-D-glucuronate + NAD⁺ = UDP-β-L-threo-pentapyranos-4-ulose + CO₂ + NADH + H⁺

For diagram of UDP-4-amino-4-deoxy-β-L-arabinose biosynthesis, click here

Other name(s):

UDP-GlcUA decarboxylase; ArnADH; UDP-glucuronate:NAD⁺ oxidoreductase (decarboxylating)

Systematic name:

UDP-α-D-glucuronate:NAD⁺ oxidoreductase (decarboxylating)

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:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Breazeale, S.D., Ribeiro, A.A., McClerren, A.L. and Raetz, C.R.H. 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 (2005) 14154–14167. [DOI] [PMID: 15695810]
2.	Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. 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 (2004) 13370–13379. [DOI] [PMID: 15491143]
3.	Williams, G.J., Breazeale, S.D., Raetz, C.R.H. and Naismith, J.H. 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 (2005) 23000–23008. [DOI] [PMID: 15809294]
4.	Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance. Structure 13 (2005) 929–942. [DOI] [PMID: 15939024]
5.	Yan, A., Guan, Z. and Raetz, C.R.H. An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli. J. Biol. Chem. 282 (2007) 36077–36089. [DOI] [PMID: 17928292]

[EC 1.1.1.305 created 2010]