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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Escherichia coli K-12 substr. MG1655 Reaction: 1.16.1.9

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.16.1.9

Enzymes and Genes:
ferric reductase, NADPH-dependent Inferred from experiment : yqjH

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: ferric-chelate reductase (NADPH)

Enzyme Commission Synonyms: ferric chelate reductase (ambiguous), iron chelate reductase (ambiguous), NADPH:Fe3+-EDTA reductase, NADPH-dependent ferric reductase, yqjH (gene name), Fe(II):NADP+ oxidoreductase

Enzyme Commission Summary:
Contains FAD. The reaction is catalysed in the reverse direction. The enzyme, which is widespread among bacteria, catalyses the reduction and release of iron from a variety of iron chelators (siderophores), including ferric triscatecholates and ferric dicitrate. The enzyme from Escherichia coli has the highest efficiency with the hydrolysed ferric enterobactin complex ferric N-(2,3-dihydroxybenzoyl)-L-serine [Miethke11].

Citations: [Bamford08, Wang11d]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.16.1.9 , ENZYME:EC:1.16.1.9 , IUBMB-ExplorEnz:EC:1.16.1.9

Credits:
Created 28-Nov-2011 by Keseler I , SRI International


References

Bamford08: Bamford VA, Armour M, Mitchell SA, Cartron M, Andrews SC, Watson KA (2008). "Preliminary X-ray diffraction analysis of YqjH from Escherichia coli: a putative cytoplasmic ferri-siderophore reductase." Acta Crystallogr Sect F Struct Biol Cryst Commun 64(Pt 9);792-6. PMID: 18765906

Miethke11: Miethke M, Hou J, Marahiel MA (2011). "The siderophore-interacting protein YqjH acts as a ferric reductase in different iron assimilation pathways of Escherichia coli." Biochemistry 50(50);10951-64. PMID: 22098718

Wang11d: Wang S, Wu Y, Outten FW (2011). "Fur and the novel regulator YqjI control transcription of the ferric reductase gene yqjH in E. coli." J Bacteriol 193(2):563-74. PMID: 21097627


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, biocyc14.