Literature summary for 2.4.2.53 extracted from

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 (2005), J. Biol. Chem., 280, 14154-14167.

Search for more literature for 2.4.2.53

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-4-deoxy-4-formamido-beta-L-arabinopyranose + ditrans,polycis-undecaprenyl phosphate	-	Escherichia coli	UDP + 4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans,polycis-undecaprenyl phosphate	-	?

Synonyms

Synonyms	Comment	Organism
ArnC	-	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	enzyme takes part in the biosynthesis of UDP-4-amino-4-deoxy-L-arabinose in polymyxin-resistant Escherichia coli. The N-formylation of UDP-4-amino-4-deoxy-L-arabinose is an obligatory step in the biosynthesis of 4-amino-4-deoxy-L-arabinose-modified lipid A in polymyxin-resistant mutants. Only the formylated sugar nucleotide is converted in vitro to an undecaprenyl phosphate-linked form by the enzyme ArnC. Because the L-Ara4N unit attached to lipid A is not derivatized with a formyl group, a deformylase must be acting later in the pathway	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)