View source for UDP-4-amino-4-deoxy-L-arabinose formyltransferase

{{Short description|Class of enzymes}}
{{Infobox enzyme
| Name       = UDP-4-amino-4-deoxy-L-arabinose formyltransferase
| EC_number  = 2.1.2.13
| CAS_number =
| GO_code    = 
| image      = 
| width      = 
| caption    =  
}}
'''UDP-4-amino-4-deoxy-L-arabinose formyltransferase''' ({{EC number|2.1.2.13}}, ''UDP-L-Ara4N formyltransferase'', ''ArnAFT'') is an [[enzyme]] with [[List of enzymes|systematic name]] ''10-formyltetrahydrofolate:UDP-4-amino-4-deoxy-beta-L-arabinose N-formyltransferase''.<ref>{{cite journal | vauthors = Breazeale SD, Ribeiro AA, McClerren AL, Raetz CR | title = 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 | journal = The Journal of Biological Chemistry | volume = 280 | issue = 14 | pages = 14154–67 | date = April 2005 | pmid = 15695810 | doi = 10.1074/jbc.M414265200 | doi-access =  free}}</ref><ref>{{cite journal | vauthors = Gatzeva-Topalova PZ, May AP, Sousa MC | title = 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 | journal = Biochemistry | volume = 44 | issue = 14 | pages = 5328–38 | date = April 2005 | pmid = 15807526 | pmc = 2583347 | doi = 10.1021/bi047384g }}</ref><ref>{{cite journal | vauthors = Williams GJ, Breazeale SD, Raetz CR, Naismith JH | title = Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis | journal = The Journal of Biological Chemistry | volume = 280 | issue = 24 | pages = 23000–8 | date = June 2005 | pmid = 15809294 | pmc = 3326539 | doi = 10.1074/jbc.M501534200 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Gatzeva-Topalova PZ, May AP, Sousa MC | title = Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance | journal = Structure | volume = 13 | issue = 6 | pages = 929–42 | date = June 2005 | pmid = 15939024 | pmc = 2997725 | doi = 10.1016/j.str.2005.03.018 }}</ref><ref>{{cite journal | vauthors = Yan A, Guan Z, Raetz CR | title = An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli | journal = The Journal of Biological Chemistry | volume = 282 | issue = 49 | pages = 36077–89 | date = December 2007 | pmid = 17928292 | pmc = 2613183 | doi = 10.1074/jbc.M706172200 | doi-access = free }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]

: [[10-formyltetrahydrofolate]] + UDP-4-amino-4-deoxy-beta-L-arabinopyranose <math>\rightleftharpoons</math> [[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 ==
{{reflist}}

== External links ==
* {{MeshName|UDP-4-amino-4-deoxy-L-arabinose+formyltransferase}}

{{One carbon transferases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}

[[Category:EC 2.1.2]]