UDP-glucuronska kiselina dehidrogenaza

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UDP-glucuronska kiselina dehidrogenaza
Identifikatori
EC broj 1.1.1.305
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum

UDP-glucuronska kiselina dehidrogenaza (EC 1.1.1.305, UDP-GlcUA dekarboksilaza, ArnADH) je enzim sa sistematskim imenom UDP-glukuronat:NAD+ oksidoreduktaza (dekarboksilacija).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju

UDP-glukuronat + NAD+ UDP-beta-L-treo-pentapiranoz-4-uloza + CO2 + NADH + H+

Ova dehidrogenaza je deo bifunkcionalnog enzima koji takođe izvodi reakciju EC 2.1.2.13, UDP-4-amino-4-dezoksi-L-arabinoza formiltransferaza.

Reference[uredi | uredi kod]

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

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