Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
twitter

Escherichia coli K-12 substr. MG1655 Reaction: 1.16.1.9


Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 1.16.1.9

Enzymes and Genes:
ferric reductase, NADPH-dependentInferred 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 direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. 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, Wang11c]

Gene-Reaction Schematic

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

Wang11c: Wang S, Wu Y, Outten FW (2011). "Fur and the novel regulator YqjI control transcription of the ferric reductase gene yqjH in Escherichia 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 Pathway Tools version 19.5 (software by SRI International) on Wed Feb 10, 2016, biocyc13.