Biology:UDP-4-amino-4-deoxy-L-arabinose formyltransferase
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Short description: Class of enzymes
| 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
- ↑ "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. April 2005. doi:10.1074/jbc.M414265200. PMID 15695810.
- ↑ "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. April 2005. doi:10.1021/bi047384g. PMID 15807526.
- ↑ "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. June 2005. doi:10.1074/jbc.M501534200. PMID 15809294.
- ↑ "Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance". Structure 13 (6): 929–42. June 2005. doi:10.1016/j.str.2005.03.018. PMID 15939024.
- ↑ "An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli". The Journal of Biological Chemistry 282 (49): 36077–89. December 2007. doi:10.1074/jbc.M706172200. PMID 17928292.
External links
- UDP-4-amino-4-deoxy-L-arabinose+formyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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