EC 2.1.2.13 - UDP-4-amino-4-deoxy-L-arabinose formyltransferase

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IntEnz Enzyme Nomenclature
EC 2.1.2.13

Names

Accepted name:
UDP-4-amino-4-deoxy-L-arabinose formyltransferase
Other names:
UDP-L-Ara4N formyltransferase
ArnAFT
Systematic name:
10-formyltetrahydrofolate:UDP-4-amino-4-deoxy-β-L-arabinose N-formyltransferase

Reaction

Comments:

The activity is part of a bifunctional enzyme also performing the reaction of EC 1.1.1.305 [UDP-glucuronate acid oxidase (UDP-4-keto-hexauronate decarboxylating)].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0099619
UniProtKB/Swiss-Prot: (75) [show] [UniProt]

References

  1. Breazeale, S. D., Ribeiro, A. A., McClerren, A. L., Raetz, C. R.
    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 (2005). [PMID: 15695810]
  2. Gatzeva-Topalova, P. Z., May, A. P., Sousa, M. C.
    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 : 5328-5338 (2005). [PMID: 15807526]
  3. Williams, G. J., Breazeale, S. D., Raetz, C. R., Naismith, J. H.
    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 (2005). [PMID: 15809294]
  4. Gatzeva-Topalova, P. Z., May, A. P., Sousa, M. C.
    Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance.
    Structure 13 : 929-942 (2005). [PMID: 15939024]
  5. Yan, A., Guan, Z., Raetz, C. R.
    An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli.
    J. Biol. Chem. 282 : 36077-36089 (2007). [PMID: 17928292]

[EC 2.1.2.13 created 2010]