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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
low Mg2+/Ca2+ concentration of 1 mM and a pH decrease from 8 to 6 both induce polymyxin resistance. Transcription of the pmrF operon in Yersinia pseudotuberculosis increases accordingly, by a factor of 7 and 2.5 for the Mg2+/Ca2+ ion starvation and acidic pH conditions, respectively
pmrF expression is independent of polymyxin resistance proteins PmrA-PmrB in Yersinia pseudotuberculosis, with the response regulator PhoP interacting directly with the pmrF operon promoter region
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
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
Marceau, M.; Sebbane, F.; Ewann, F.; Collyn, F.; Lindner, B.; Campos, M.A.; Bengoechea, J.A.; Simonet, M.
The pmrF polymyxin-resistance operon of Yersinia pseudotuberculosis is upregulated by the PhoP-PhoQ two-component system but not by PmrA-PmrB, and is not required for virulence
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