Stereospecificity of the ferric enterobactin receptor of Escherichia coli K-12.
Synthetic enterobactin and enantioenterobactin (D-seryl enterobactin) have been examined for the ability to transport iron in Escherichia coli. Failure of the unnatural, D-serine-derived material to support growth of E. coli mutants indicates outer membrane receptor specificity for the naturally occurring complex having an L-seryl backbone and the delta-cis configuration of the Fe(III).catecholate center. Enantioenterobactin was markedly less effective in protecting cells against colicin B compared to synthetic or natural enterobactin.
D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins / Q000378:metabolism*; D004758:Enterobactin / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D011956:Receptors, Cell Surface; D012694:Serine / Q000031:analogs & derivatives*; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D011956:Receptors, Cell Surface; C029489:enterobactin receptor; D004758:Enterobactin; D012694:Serine