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MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655: UDP-L-Ara4N formyltransferaseInferred from experiment: arnA

In Pathway: polymyxin resistance

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: UDP-4-amino-4-deoxy-L-arabinose formyltransferase

Enzyme Commission Synonyms: UDP-L-Ara4N formyltransferase, ArnAFT

Standard Gibbs Free Energy (ΔrG in kcal/mol): 16.471832Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The activity is part of a bifunctional enzyme also performing the reaction of EC [UDP-glucuronic acid oxidase (UDP-4-keto-hexauronic acid decarboxylating)].

Citations: [Breazeale02, Breazeale05, GatzevaTopalova05, Williams05, GatzevaTopalova05a, Yan07]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R07660, Rhea:24706

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:

Revised 12-Mar-2010 by Caspi R, SRI International


Breazeale02: Breazeale SD, Ribeiro AA, Raetz CR (2002). "Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose." J Biol Chem 277(4);2886-96. PMID: 11706007

Breazeale05: Breazeale SD, Ribeiro AA, McClerren AL, Raetz CR (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(14);14154-67. PMID: 15695810

GatzevaTopalova05: Gatzeva-Topalova PZ, May AP, Sousa MC (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. PMID: 15807526

GatzevaTopalova05a: Gatzeva-Topalova PZ, May AP, Sousa MC (2005). "Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance." Structure (Camb) 13(6);929-42. PMID: 15939024

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Williams05: Williams GJ, Breazeale SD, Raetz CR, Naismith JH (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(24);23000-8. PMID: 15809294

Yan07: Yan A, Guan Z, Raetz CR (2007). "An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli." J Biol Chem 282(49);36077-89. PMID: 17928292

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Fri Feb 12, 2016, biocyc12.