2.0 2012-07-30 14:55:30 -0600 2015-06-03 17:21:15 -0600 ECMDB21372 M2MDB001768 Ferric enterobactin Ferric 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-enterobactin Fe-enterochlin Ferric 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) C30H33FeN3O15 731.439 731.126109534 N-[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 iron N-[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=C1 InChI=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-N Membrane logp 4.16 ChemAxon pka_strongest_acidic 6.54 ChemAxon pka_strongest_basic -6.3 ChemAxon iupac N-[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 iron ChemAxon average_mass 731.439 ChemAxon mono_mass 731.126109534 ChemAxon smiles [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=C1 ChemAxon formula C30H33FeN3O15 ChemAxon inchi InChI=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); ChemAxon inchikey WPYKFMKTUGWUGY-UHFFFAOYSA-N ChemAxon polar_surface_area 307.53 ChemAxon refractivity 162.87 ChemAxon polarizability 65.12 ChemAxon rotatable_bond_count 6 ChemAxon acceptor_count 18 ChemAxon donor_count 12 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Biosynthesis of siderophore group nonribosomal peptides 2,3-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. PW000760 ec01053 Metabolic inner membrane transport list 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 added PW000786 Metabolic Specdb::CMs 1084492 Specdb::NmrOneD 272318 Specdb::NmrOneD 272319 Specdb::NmrOneD 272320 Specdb::NmrOneD 272321 Specdb::NmrOneD 272322 Specdb::NmrOneD 272323 Specdb::NmrOneD 272324 Specdb::NmrOneD 272325 Specdb::NmrOneD 272326 Specdb::NmrOneD 272327 Specdb::NmrOneD 272328 Specdb::NmrOneD 272329 Specdb::NmrOneD 272330 Specdb::NmrOneD 272331 Specdb::NmrOneD 272332 Specdb::NmrOneD 272333 Specdb::NmrOneD 272334 Specdb::NmrOneD 272335 Specdb::NmrOneD 272336 Specdb::NmrOneD 272337 Specdb::MsMs 26282 Specdb::MsMs 26283 Specdb::MsMs 26284 Specdb::MsMs 32840 Specdb::MsMs 32841 Specdb::MsMs 32842 440956 389783 C06230 FERRIC-ENTEROBACTIN-COMPLEX Payne, 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. 9268330 Sprencel, 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. 10986237 Cao, 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. 10998164 Barnard, 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. 11532122 Liu, 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. 7947735 Liu, 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. 7504275 Enterochelin esterase P13039 FES_ECOLI fes http://ecmdb.ca/proteins/P13039.xml Ferric enterobactin transport ATP-binding protein fepC P23878 FEPC_ECOLI fepC http://ecmdb.ca/proteins/P23878.xml Ferric enterobactin transport system permease protein fepD P23876 FEPD_ECOLI fepD http://ecmdb.ca/proteins/P23876.xml Ferric enterobactin transport system permease protein fepG P23877 FEPG_ECOLI fepG http://ecmdb.ca/proteins/P23877.xml Ferrienterobactin-binding periplasmic protein P0AEL6 FEPB_ECOLI fepB http://ecmdb.ca/proteins/P0AEL6.xml Ferric enterobactin transport ATP-binding protein fepC P23878 FEPC_ECOLI fepC http://ecmdb.ca/proteins/P23878.xml Ferric enterobactin transport system permease protein fepD P23876 FEPD_ECOLI fepD http://ecmdb.ca/proteins/P23876.xml Ferric enterobactin transport system permease protein fepG P23877 FEPG_ECOLI fepG http://ecmdb.ca/proteins/P23877.xml Ferrienterobactin-binding periplasmic protein P0AEL6 FEPB_ECOLI fepB http://ecmdb.ca/proteins/P0AEL6.xml Biopolymer transport protein exbB P0ABU7 EXBB_ECOLI exbB http://ecmdb.ca/proteins/P0ABU7.xml Biopolymer transport protein exbD P0ABV2 EXBD_ECOLI exbD http://ecmdb.ca/proteins/P0ABV2.xml Ferrienterobactin receptor P05825 FEPA_ECOLI fepA http://ecmdb.ca/proteins/P05825.xml Protein tonB P02929 TONB_ECOLI tonB http://ecmdb.ca/proteins/P02929.xml Adenosine triphosphate + Water + Ferric enterobactin > ADP + Ferric enterobactin + Hydrogen ion + Phosphate ABC-10-RXN Adenosine triphosphate + Water + Ferric enterobactin > ADP + Ferric enterobactin + Hydrogen ion + Phosphate ABC-10-RXN Ferric enterobactin + 3 Water >3 2,3-Dihydroxybenzoylserine + Fe3+ +3 Hydrogen ion Enterochelin + Fe3+ > Ferric enterobactin Ferric enterobactin + Water > ferric 2,3-dihydroxybenzoylserine RXN0-6938 Adenosine triphosphate + Ferric enterobactin + Water > ADP + Phosphate + Ferric enterobactin + Hydrogen ion ABC-10-RXN Adenosine triphosphate + Ferric enterobactin + Water > ADP + Phosphate + Ferric enterobactin + Hydrogen ion ABC-10-RXN Ferric enterobactin + Adenosine triphosphate + Water Ferric enterobactin + Adenosine diphosphate + Hydrogen ion + ADP PW_RCT000137 Ferric enterobactin + Adenosine triphosphate + Water Ferric enterobactin + Adenosine diphosphate + Hydrogen ion + ADP PW_RCT000137