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Class of enzymes
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
⇌
{\displaystyle \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.
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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 .
Activity Regulation Classification Kinetics Types