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

10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose

\rightleftharpoons

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

↑ 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.
↑ 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. PMID 15807526.
↑ 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 3326539. PMID 15809294.
↑ 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 2997725. PMID 15939024.
↑ 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 2613183. PMID 17928292.

External links

UDP-4-amino-4-deoxy-L-arabinose formyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)

Transferase: one carbon transferases (EC 2.1)

2.1.1: Methyl-

N-	Histamine N-methyltransferase Phenylethanolamine N-methyltransferase Amine N-methyltransferase Phosphatidylethanolamine N-methyltransferase

O-	5-hydroxyindole-O-methyltransferase/Acetylserotonin O-methyltransferase Catechol-O-methyl transferase

Homocysteine	Betaine-homocysteine methyltransferase Homocysteine methyltransferase Methionine synthase

Other	Phosphatidyl ethanolamine methyltransferase DNMT3B Histone methyltransferase Thymidylate synthase DNA methyltransferase Thiopurine methyltransferase

2.1.2: Hydroxymethyl-,
Formyl- and Related

Hydroxymethyltransferase	Serine hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase

Formyltransferase	Phosphoribosylglycinamide formyltransferase Inosine monophosphate synthase

Other	Glutamate formimidoyltransferase Aminomethyltransferase

2.1.3: Carboxy-
and Carbamoyl

Carboxy	methylmalonyl-CoA carboxytransferase

Carbamoyl	Aspartate carbamoyltransferase Ornithine carbamoyltransferase Oxamate carbamoyltransferase Putrescine carbamoyltransferase 3-hydroxymethylcephem carbamoyltransferase Lysine carbamoyltransferase N-acetylornithine carbamoyltransferase

2.1.4: Amidine

Arginine:glycine amidinotransferase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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