Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase

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Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
Identifiers
EC no. 2.7.8.30
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Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase (EC 2.7.8.30, undecaprenyl-phosphate Ara4FN transferase, Ara4FN transferase, polymyxin resistance protein PmrF, UDP-4-amino-4-deoxy-alpha-L-arabinose:ditrans,polycis-undecaprenyl phosphate 4-amino-4-deoxy-alpha-L-arabinosyltransferase) is an enzyme with systematic name UDP-4-amino-4-deoxy-alpha-L-arabinose:ditrans,octacis-undecaprenyl phosphate 4-amino-4-deoxy-alpha-L-arabinosyltransferase. [1] [2] This enzyme catalyses the following chemical reaction

UDP-4-deoxy-4-formamido-beta-L-arabinopyranose + ditrans, octacis-undecaprenyl phosphate UDP + 4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans, octacis-undecaprenyl phosphate

The enzyme shows no activity with UDP-4-amino-4-deoxy-beta-L-arabinose.

Related Research Articles

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In molecular biology, the lipopolysaccharide kinase (Kdo/WaaP) family is a family of lipopolysaccharide kinases that includes lipopolysaccharide core heptose(I) kinase rfaP. Lipopolysaccharide core heptose(I) kinase rfaP is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that it is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of Salmonella enterica. The family also includes 3-deoxy-D-manno-octulosonic acid kinase from Haemophilus influenzae, which phosphorylates Kdo-lipid IV(A), a lipopolysaccharide precursor, and is involved in virulence.

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UDP-N-acetylglucosamine---decaprenyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:trans,octacis-decaprenyl-phosphate N-acetylglucosaminephosphotransferase. This enzyme catalyses the following chemical reaction

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The enterobacterial common antigen (ECA) is a carbohydrate antigen found in the outer membrane of many Enterobacterales species. The antigen is unanimously absent from other gram-negative and gram-positive bacteria. Aeromonas hydrophila 209A is the only organism outside of Enterobacterales that expresses the ECA. More studies are needed to explain the presence of the antigen in this species as no other strains of this species express the antigen. The ECA is a polysaccharide made of repeating units of trisaccharides. The functions of these units have very few proven functions. Some evidence indicates role in pathogenicity in the bacteria that present the ECA. There are three separate types of ECA these include ECAPG, ECALPS, and ECACYC, each have different lengths. The synthesis of the ECA is controlled by the wec operon and has a 12-step synthesis which is described below. Due to the lack of proven function of the ECA, any clinical significance is hard to define however, some evidence suggests that human serum has antibodies against ECA.

References

  1. ↑ Breazeale SD, Ribeiro AA, Raetz CR (January 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". The Journal of Biological Chemistry. 277 (4): 2886–96. doi: 10.1074/jbc.M109377200 . PMID   11706007.
  2. ↑ Breazeale SD, Ribeiro AA, McClerren AL, Raetz CR (April 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". The Journal of Biological Chemistry. 280 (14): 14154–67. doi: 10.1074/jbc.M414265200 . PMID   15695810.
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