|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 22.214.171.124
Enzymes and Genes:
|Escherichia coli K-12 substr. MG1655 :||UDP-L-Ara4N formyltransferase
In Pathway: polymyxin resistance
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. 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): 16.471832 [Latendresse13]
Enzyme Commission Summary:
The activity is part of a bifunctional enzyme also performing the reaction of EC 126.96.36.1995 [UDP-glucuronic acid oxidase (UDP-4-keto-hexauronic acid decarboxylating)].
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). "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
GatzevaTopalova05a: 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
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
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493