2.02012-07-30 14:55:30 -06002015-06-03 17:21:15 -0600ECMDB21372M2MDB001768Ferric enterobactinFerric enterobactin is a member of the chemical class known as Catechols. These are compounds containing a 1,2-benzenediol moeity. Ferric enterobactin is a catecholate siderophore that binds with high affinity (Kd approximately 10-10 M) to the Escherichia coli outer membrane protein FepA. (PMID 10998164) The Escherichia coli FepA protein is an energy- and TonB-dependent, ligand-binding porin that functions as a receptor for the siderophore ferric enterobactin and colicins B and D. (PMID 9268330) The periplasmic protein FepB of Escherichia coli is a component of the ferric enterobactin transport system. (PMID 10986237) The ferric enterobactin receptor, FepA, is a TonB-dependent gated porin that transports the siderophore ferric enterobactin across the outer membrane of gram-negative bacteria. (PMID 7947735) In Escherichia coli, the outer membrane protein FepA is a receptor for the siderophore complex ferric enterobactin and for colicins B and D. (PMID 2201687) FepA is an Escherichia coli outer membrane receptor protein for the siderophore ferric enterobactin. (PMID 7504275) FepA is the Escherichia coli outer membrane receptor for ferric enterobactin, colicin D and colicin B. (PMID 11532122)Fe-enterobactinFe-enterochlinFerric enterobactin complex[Fe(ent)]3{N,N',N''-[(3S,7S,11S)-2,6,10-trioxo-1,5,9-trioxacyclododecane-3,7,11-triyl]tris[2,3-di(hydroxy-kappaO)benzamidato]}ferrate(3){N,n',n''-[(3S,7S,11S)-2,6,10-trioxo-1,5,9-trioxacyclododecane-3,7,11-triyl]tris[2,3-di(hydroxy-kappao)benzamidato]}ferric acid(3)C30H33FeN3O15731.439731.126109534N-[7,11-bis({[(2,3-dihydroxyphenyl)(hydroxy)methylidene]amino})-2,6,10-trihydroxy-1,5,9-trioxacyclododecan-3-yl]-2,3-dihydroxybenzene-1-carboximidic acid ironN-[7,11-bis({[(2,3-dihydroxyphenyl)(hydroxy)methylidene]amino})-2,6,10-trihydroxy-1,5,9-trioxacyclododecan-3-yl]-2,3-dihydroxybenzenecarboximidic acid iron[Fe].OC1OCC(N=C(O)C2=C(O)C(O)=CC=C2)C(O)OCC(N=C(O)C2=C(O)C(O)=CC=C2)C(O)OCC1N=C(O)C1=C(O)C(O)=CC=C1InChI=1S/C30H33N3O15.Fe/c34-19-7-1-4-13(22(19)37)25(40)31-16-10-46-29(44)18(33-27(42)15-6-3-9-21(36)24(15)39)12-48-30(45)17(11-47-28(16)43)32-26(41)14-5-2-8-20(35)23(14)38;/h1-9,16-18,28-30,34-39,43-45H,10-12H2,(H,31,40)(H,32,41)(H,33,42);WPYKFMKTUGWUGY-UHFFFAOYSA-NMembranelogp4.16pka_strongest_acidic6.54pka_strongest_basic-6.3iupacN-[7,11-bis({[(2,3-dihydroxyphenyl)(hydroxy)methylidene]amino})-2,6,10-trihydroxy-1,5,9-trioxacyclododecan-3-yl]-2,3-dihydroxybenzene-1-carboximidic acid ironaverage_mass731.439mono_mass731.126109534smiles[Fe].OC1OCC(N=C(O)C2=C(O)C(O)=CC=C2)C(O)OCC(N=C(O)C2=C(O)C(O)=CC=C2)C(O)OCC1N=C(O)C1=C(O)C(O)=CC=C1formulaC30H33FeN3O15inchiInChI=1S/C30H33N3O15.Fe/c34-19-7-1-4-13(22(19)37)25(40)31-16-10-46-29(44)18(33-27(42)15-6-3-9-21(36)24(15)39)12-48-30(45)17(11-47-28(16)43)32-26(41)14-5-2-8-20(35)23(14)38;/h1-9,16-18,28-30,34-39,43-45H,10-12H2,(H,31,40)(H,32,41)(H,33,42);inchikeyWPYKFMKTUGWUGY-UHFFFAOYSA-Npolar_surface_area307.53refractivity162.87polarizability65.12rotatable_bond_count6acceptor_count18donor_count12physiological_charge0formal_charge0Biosynthesis of siderophore group nonribosomal peptides2,3-dihydroxybenzoate is synthesized from chorismate via isochorismate and 2,3-dihydroxy-2,3-dihydrobenzoate.
The biosynthesis of 2,3-dihydroxybenzoate starts from chorismate being synthesized into isochorismate through isochorismate synthase entC. EntC catalyzes the conversion of chorismate to isochorismate. The N-terminal isochorismate lyase domain of EntB hydrolyzes the pyruvate group of isochorismate to produce 2,3-dihydro-2,3-dihydroxybenzoate. The conversion of this latter compound to 2,3-dihydroxybenzoate is catalyzed by the EntA dehydrogenase.This compound then interacts with L-serine and ATP through enterobactin synthase protein complex resulting in the production of enterobactin. Enterobactin is exported into the periplasmic space through the enterobactin exporter entS. The compound is the export to the environment through the outer membrane protein TolC. In the environment enterobactin reacts with iron to produce Ferric enterobactin. This compound is imported into the periplasmic space through a ferric enterobactin outermembrane transport complex. The compound then enters the cytoplasm through a ferric enterobactin ABC transporter.Once inside the cytoplasm, ferric enterobactin spontaneously releases the iron ion from the enterobactin.
PW000760ec01053Metabolicinner membrane transportlist of inner membrane transport complexes, transporting compounds from the periplasmic space to the cytosol
This pathway should be updated regularly with the new inner membrae transports addedPW000786MetabolicSpecdb::CMs1084492Specdb::NmrOneD272318Specdb::NmrOneD272319Specdb::NmrOneD272320Specdb::NmrOneD272321Specdb::NmrOneD272322Specdb::NmrOneD272323Specdb::NmrOneD272324Specdb::NmrOneD272325Specdb::NmrOneD272326Specdb::NmrOneD272327Specdb::NmrOneD272328Specdb::NmrOneD272329Specdb::NmrOneD272330Specdb::NmrOneD272331Specdb::NmrOneD272332Specdb::NmrOneD272333Specdb::NmrOneD272334Specdb::NmrOneD272335Specdb::NmrOneD272336Specdb::NmrOneD272337Specdb::MsMs26282Specdb::MsMs26283Specdb::MsMs26284Specdb::MsMs32840Specdb::MsMs32841Specdb::MsMs32842440956389783C06230FERRIC-ENTEROBACTIN-COMPLEXPayne, M. A., Igo, J. D., Cao, Z., Foster, S. B., Newton, S. M., Klebba, P. E. (1997). "Biphasic binding kinetics between FepA and its ligands." J Biol Chem 272:21950-21955.9268330Sprencel, C., Cao, Z., Qi, Z., Scott, D. C., Montague, M. A., Ivanoff, N., Xu, J., Raymond, K. M., Newton, S. M., Klebba, P. E. (2000). "Binding of ferric enterobactin by the Escherichia coli periplasmic protein FepB." J Bacteriol 182:5359-5364.10986237Cao, Z., Qi, Z., Sprencel, C., Newton, S. M., Klebba, P. E. (2000). "Aromatic components of two ferric enterobactin binding sites in Escherichia coli FepA." Mol Microbiol 37:1306-1317.10998164Barnard, T. J., Watson, M. E. Jr, McIntosh, M. A. (2001). "Mutations in the Escherichia coli receptor FepA reveal residues involved in ligand binding and transport." Mol Microbiol 41:527-536.11532122Liu, J., Rutz, J. M., Klebba, P. E., Feix, J. B. (1994). "A site-directed spin-labeling study of ligand-induced conformational change in the ferric enterobactin receptor, FepA." Biochemistry 33:13274-13283.7947735Liu, J., Rutz, J. M., Feix, J. B., Klebba, P. E. (1993). "Permeability properties of a large gated channel within the ferric enterobactin receptor, FepA." Proc Natl Acad Sci U S A 90:10653-10657.7504275Enterochelin esteraseP13039FES_ECOLIfeshttp://ecmdb.ca/proteins/P13039.xmlFerric enterobactin transport ATP-binding protein fepCP23878FEPC_ECOLIfepChttp://ecmdb.ca/proteins/P23878.xmlFerric enterobactin transport system permease protein fepDP23876FEPD_ECOLIfepDhttp://ecmdb.ca/proteins/P23876.xmlFerric enterobactin transport system permease protein fepGP23877FEPG_ECOLIfepGhttp://ecmdb.ca/proteins/P23877.xmlFerrienterobactin-binding periplasmic proteinP0AEL6FEPB_ECOLIfepBhttp://ecmdb.ca/proteins/P0AEL6.xmlFerric enterobactin transport ATP-binding protein fepCP23878FEPC_ECOLIfepChttp://ecmdb.ca/proteins/P23878.xmlFerric enterobactin transport system permease protein fepDP23876FEPD_ECOLIfepDhttp://ecmdb.ca/proteins/P23876.xmlFerric enterobactin transport system permease protein fepGP23877FEPG_ECOLIfepGhttp://ecmdb.ca/proteins/P23877.xmlFerrienterobactin-binding periplasmic proteinP0AEL6FEPB_ECOLIfepBhttp://ecmdb.ca/proteins/P0AEL6.xmlBiopolymer transport protein exbBP0ABU7EXBB_ECOLIexbBhttp://ecmdb.ca/proteins/P0ABU7.xmlBiopolymer transport protein exbDP0ABV2EXBD_ECOLIexbDhttp://ecmdb.ca/proteins/P0ABV2.xmlFerrienterobactin receptorP05825FEPA_ECOLIfepAhttp://ecmdb.ca/proteins/P05825.xmlProtein tonBP02929TONB_ECOLItonBhttp://ecmdb.ca/proteins/P02929.xmlAdenosine triphosphate + Water + Ferric enterobactin > ADP + Ferric enterobactin + Hydrogen ion + PhosphateABC-10-RXNAdenosine triphosphate + Water + Ferric enterobactin > ADP + Ferric enterobactin + Hydrogen ion + PhosphateABC-10-RXNFerric enterobactin + 3 Water >3 2,3-Dihydroxybenzoylserine + Fe3+ +3 Hydrogen ionEnterochelin + Fe3+ > Ferric enterobactinFerric enterobactin + Water > ferric 2,3-dihydroxybenzoylserineRXN0-6938Adenosine triphosphate + Ferric enterobactin + Water > ADP + Phosphate + Ferric enterobactin + Hydrogen ionABC-10-RXNAdenosine triphosphate + Ferric enterobactin + Water > ADP + Phosphate + Ferric enterobactin + Hydrogen ionABC-10-RXNFerric enterobactin + Adenosine triphosphate + Water Ferric enterobactin + Adenosine diphosphate + Hydrogen ion + ADPPW_RCT000137Ferric enterobactin + Adenosine triphosphate + Water Ferric enterobactin + Adenosine diphosphate + Hydrogen ion + ADPPW_RCT000137