Record Information
Version2.0
Creation Date2012-05-31 14:48:35 -0600
Update Date2015-06-03 17:20:08 -0600
Secondary Accession Numbers
  • ECMDB20516
Identification
Name:Ferric coprogen
DescriptionFerric coprogen belongs to the class of Fatty Acid Esters. These are carboxylic ester derivatives of a fatty acid. (inferred from compound structure)Coprogen is involved in iron transportation. The FhuE protein of Escherichia coli functions as the receptor for ferric coprogen and ferric-rhodotorulic acid. (PMID 3032906) The fhuE gene of Escherichia coli encodes the FhuE protein, which is a receptor protein in the coprogen-mediated siderophore iron-transport system. (PMID 16502288) Removal of iron from coprogen, ferrichrome, and ferrioxamine B was significantly lower in fhuF mutants compared to the corresponding parental strains, which suggested that FhuF is involved in iron removal from these hydroxamate-type siderophores. (PMID 14756576) Insertional inactivation and gene replacement of both genes showed that while FhuD2 is involved in the transport of iron(III) in complex with ferrichrome, ferrioxamine B, aerobactin, and coprogen, FhuD1 shows a more limited substrate range, capable of only iron(III)-ferrichrome and iron(III)-ferrioxamine B transport in S. (PMID 11489851)
Structure
Thumb
Synonyms:
  • Coprogen
Chemical Formula:C35H53FeN6O13
Weight:Average: 821.673
Monoisotopic: 821.302002945
InChI Key:FQIVLXIUJLOKPL-QYOPVWIVSA-N
InChI:InChI=1S/C35H53N6O13.Fe/c1-23(11-17-42)20-30(45)39(51)14-5-8-27-33(48)38-28(34(49)37-27)9-6-15-40(52)32(47)22-25(3)13-19-54-35(50)29(36-26(4)44)10-7-16-41(53)31(46)21-24(2)12-18-43;/h20-22,27-29,42-43H,5-19H2,1-4H3,(H,36,44)(H,37,49)(H,38,48);/q-3;+3/b23-20-,24-21+,25-22-;
CAS number:31418-71-0
IUPAC Name:iron(3+) ion N-(1-{[(3Z)-4-{[3-(3,6-dihydroxy-5-{3-[(2Z)-5-hydroxy-3-methyl-N-oxidopent-2-enamido]propyl}-2,5-dihydropyrazin-2-yl)propyl](oxido)carbamoyl}-3-methylbut-3-en-1-yl]oxy}-5-[(2E)-5-hydroxy-3-methyl-N-oxidopent-2-enamido]-1-oxopentan-2-yl)ethanimidic acid
Traditional IUPAC Name:iron(3+) ion N-(1-{[(3Z)-4-{[3-(3,6-dihydroxy-5-{3-[(2Z)-5-hydroxy-3-methyl-N-oxidopent-2-enamido]propyl}-2,5-dihydropyrazin-2-yl)propyl](oxido)carbamoyl}-3-methylbut-3-en-1-yl]oxy}-5-[(2E)-5-hydroxy-3-methyl-N-oxidopent-2-enamido]-1-oxopentan-2-yl)ethanimidic acid
SMILES:[Fe+3].[H]\C(=C(\C)CCO)C(=O)N([O-])CCCC(N=C(C)O)C(=O)OCC\C(C)=C(\[H])C(=O)N([O-])CCCC1N=C(O)C(CCCN([O-])C(=O)C(\[H])=C(\C)CCO)N=C1O
Chemical Taxonomy
Description belongs to the class of organic compounds known as n-acyl-alpha amino acids and derivatives. N-acyl-alpha amino acids and derivatives are compounds containing an alpha amino acid (or a derivative thereof) which bears an acyl group at its terminal nitrogen atom.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentN-acyl-alpha amino acids and derivatives
Alternative Parents
Substituents
  • Alpha-amino acid ester
  • N-acyl-alpha amino acid or derivatives
  • Dioxopiperazine
  • 2,5-dioxopiperazine
  • Fatty acid ester
  • 1,4-diazinane
  • Piperazine
  • Fatty acyl
  • Acetamide
  • Carboxamide group
  • Carboxylic acid ester
  • Lactam
  • Secondary carboxylic acid amide
  • Organoheterocyclic compound
  • Organic transition metal salt
  • Monocarboxylic acid or derivatives
  • Azacycle
  • Organonitrogen compound
  • Hydrocarbon derivative
  • Organic nitrogen compound
  • Organic oxide
  • Organopnictogen compound
  • Organic oxygen compound
  • Organic salt
  • Alcohol
  • Organooxygen compound
  • Carbonyl group
  • Primary alcohol
  • Organic zwitterion
  • Aliphatic heteromonocyclic compound
Molecular FrameworkAliphatic heteromonocyclic compounds
External DescriptorsNot Available
Physical Properties
State:Not Available
Charge:1
Melting point:Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility0.029 g/LALOGPS
logP2.31ALOGPS
logP-0.32ChemAxon
logS-4.5ALOGPS
pKa (Strongest Acidic)5.29ChemAxon
pKa (Strongest Basic)3.6ChemAxon
Physiological Charge1ChemAxon
Hydrogen Acceptor Count15ChemAxon
Hydrogen Donor Count5ChemAxon
Polar Surface Area294.64 ŲChemAxon
Rotatable Bond Count25ChemAxon
Refractivity194.4 m³·mol⁻¹ChemAxon
Polarizability78.37 ųChemAxon
Number of Rings1ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
EcoCyc Pathways:Not Available
Concentrations
Not Available
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0uk9-1213109710-305c83889be23469ffa1View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0f79-4237029500-df24ac68df840ada3250View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0a4r-8294023000-04b77a091e6365fc39dfView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-008a-0010001900-593be6585000f38f4166View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-001m-2060001900-6ed91bdbd4ad71c97c0bView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-053u-8182203900-9af0549e149e617b9556View in MoNA
References
References:
  • Cui, Y., Tu, R., Guan, Y., Ma, L., Chen, S. (2006). "Cloning, sequencing, and characterization of the Azospirillum brasilense fhuE gene." Curr Microbiol 52:169-177. Pubmed: 16502288
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • Matzanke, B. F., Anemuller, S., Schunemann, V., Trautwein, A. X., Hantke, K. (2004). "FhuF, part of a siderophore-reductase system." Biochemistry 43:1386-1392. Pubmed: 14756576
  • Sebulsky, M. T., Heinrichs, D. E. (2001). "Identification and characterization of fhuD1 and fhuD2, two genes involved in iron-hydroxamate uptake in Staphylococcus aureus." J Bacteriol 183:4994-5000. Pubmed: 11489851
  • Yurtsever D. (2007). Fatty acid methyl ester profiling of Enterococcus and Esherichia coli for microbial source tracking. M.sc. Thesis. Villanova University: U.S.A
Synthesis Reference:Not Available
Material Safety Data Sheet (MSDS)Not Available
External Links:
ResourceLink
CHEBI IDNot Available
HMDB IDNot Available
Pubchem Compound ID6449889
Kegg IDNot Available
ChemSpider ID4952560
Wikipedia IDNot Available
BioCyc IDCPD0-621
EcoCyc IDCPD0-621

Enzymes

General function:
Involved in nucleotide binding
Specific function:
Part of the ABC transporter complex fhuCDB involved in iron(3+)-hydroxamate import. Responsible for energy coupling to the transport system
Gene Name:
fhuC
Uniprot ID:
P07821
Molecular weight:
28886
Reactions
ATP + H(2)O + iron chelate(Out) = ADP + phosphate + iron chelate(In).
General function:
Involved in transporter activity
Specific function:
Part of the ABC transporter complex fhuCDB involved in iron(3+)-hydroxamate import. Responsible for the translocation of the substrate across the membrane
Gene Name:
fhuB
Uniprot ID:
P06972
Molecular weight:
70422
General function:
Involved in binding
Specific function:
Part of the ABC transporter complex fhuCDB involved in iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and transfers it to the membrane-bound permease. Required for the transport of all iron(3+)-hydroxamate siderophores such as ferrichrome, gallichrome, desferrioxamine, coprogen, aerobactin, shizokinen, rhodotorulic acid and the antibiotic albomycin
Gene Name:
fhuD
Uniprot ID:
P07822
Molecular weight:
32998

Transporters

General function:
Involved in nucleotide binding
Specific function:
Part of the ABC transporter complex fhuCDB involved in iron(3+)-hydroxamate import. Responsible for energy coupling to the transport system
Gene Name:
fhuC
Uniprot ID:
P07821
Molecular weight:
28886
Reactions
ATP + H(2)O + iron chelate(Out) = ADP + phosphate + iron chelate(In).
General function:
Involved in transporter activity
Specific function:
Part of the ABC transporter complex fhuCDB involved in iron(3+)-hydroxamate import. Responsible for the translocation of the substrate across the membrane
Gene Name:
fhuB
Uniprot ID:
P06972
Molecular weight:
70422
General function:
Involved in receptor activity
Specific function:
Required for the uptake of Fe(3+) via coprogen, ferrioxamine B, and rhodotorulic acid
Gene Name:
fhuE
Uniprot ID:
P16869
Molecular weight:
81232
General function:
Involved in protein transporter activity
Specific function:
Involved in the tonB-dependent energy-dependent transport of various receptor-bound substrates. Protects exbD from proteolytic degradation and functionally stabilizes tonB
Gene Name:
exbB
Uniprot ID:
P0ABU7
Molecular weight:
26287
General function:
Involved in transporter activity
Specific function:
Involved in the tonB-dependent energy-dependent transport of various receptor-bound substrates
Gene Name:
exbD
Uniprot ID:
P0ABV2
Molecular weight:
15527
General function:
Involved in iron ion transmembrane transporter activity
Specific function:
Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of tonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy- dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins
Gene Name:
tonB
Uniprot ID:
P02929
Molecular weight:
26094
General function:
Involved in binding
Specific function:
Part of the ABC transporter complex fhuCDB involved in iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and transfers it to the membrane-bound permease. Required for the transport of all iron(3+)-hydroxamate siderophores such as ferrichrome, gallichrome, desferrioxamine, coprogen, aerobactin, shizokinen, rhodotorulic acid and the antibiotic albomycin
Gene Name:
fhuD
Uniprot ID:
P07822
Molecular weight:
32998