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

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

UDP-4-amino-4-deoxy-L-arabinose formyltransferase
Identifiers
EC no.2.1.2.13
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
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

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  1. ^ Breazeale SD, Ribeiro AA, McClerren AL, Raetz CR (April 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". The Journal of Biological Chemistry. 280 (14): 14154–67. doi:10.1074/jbc.M414265200. PMID 15695810.
  2. ^ Gatzeva-Topalova PZ, May AP, Sousa MC (April 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): 5328–38. doi:10.1021/bi047384g. PMC 2583347. PMID 15807526.
  3. ^ Williams GJ, Breazeale SD, Raetz CR, Naismith JH (June 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". The Journal of Biological Chemistry. 280 (24): 23000–8. doi:10.1074/jbc.M501534200. PMC 3326539. PMID 15809294.
  4. ^ Gatzeva-Topalova PZ, May AP, Sousa MC (June 2005). "Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance". Structure. 13 (6): 929–42. doi:10.1016/j.str.2005.03.018. PMC 2997725. PMID 15939024.
  5. ^ Yan A, Guan Z, Raetz CR (December 2007). "An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli". The Journal of Biological Chemistry. 282 (49): 36077–89. doi:10.1074/jbc.M706172200. PMC 2613183. PMID 17928292.
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