UDP-4-amino-4-deoxy-L-arabinose formyltransferase

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UDP-4-amino-4-deoxy-L-arabinose formyltransferase
Identifiers
EC number 2.1.2.13
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

UDP-4-amino-4-deoxy-L-arabinose formyltransferase (EC 2.1.2.13, UDP-L-Ara4N formyltransferase, ArnAFT) is an enzyme with systematic name 10-formyltetrahydrofolate:UDP-4-amino-4-deoxy-beta-L-arabinose N-formyltransferase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose

The activity is part of a bifunctional enzyme that also performs the EC 1.1.1.305 reaction.

References[edit]

  1. ^ Breazeale, S.D.; Ribeiro, A.A.; McClerren, A.L.; 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. doi:10.1074/jbc.M414265200. PMID 15695810. 
  2. ^ Gatzeva-Topalova, P.Z.; May, A.P.; Sousa, M.C. (2005). "Crystal structure and mechanism of the Escherichia coli ArnA (PmrI) transformylase domain. An enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance". Biochemistry. 44 (14): 5328–5338. doi:10.1021/bi047384g. PMC 2583347Freely accessible. PMID 15807526. 
  3. ^ Williams, G.J.; Breazeale, S.D.; Raetz, C.R.H.; 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. doi:10.1074/jbc.M501534200. PMC 3326539Freely accessible. PMID 15809294. 
  4. ^ Gatzeva-Topalova, P.Z.; May, A.P.; 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. doi:10.1016/j.str.2005.03.018. PMC 2997725Freely accessible. PMID 15939024. 
  5. ^ Yan, A.; Guan, Z.; Raetz, C.R.H. (2007). "An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli". J. Biol. Chem. 282: 36077–36089. doi:10.1074/jbc.M706172200. PMC 2613183Freely accessible. PMID 17928292. 

External links[edit]