Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 Reaction: 1.1.5.6

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

EC Number: 1.1.5.6

Enzymes and Genes:
formate dehydrogenase-O Inferred from experiment : fdoG , fdoH , fdoI
formate dehydrogenase-N Inferred from experiment : fdnG , fdnH , fdnI

In Pathway: nitrate reduction III (dissimilatory) , formate to trimethylamine N-oxide electron transfer , formate to dimethyl sulfoxide electron transfer

Note that this reaction equation differs from the official Enzyme Commission reaction equations for this EC number.

Reaction Locations: inner membrane (sensu Gram-negative Bacteria)

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: formate dehydrogenase-N

Enzyme Commission Synonyms: Fdh-N, FdnGHI, nitrate-inducible formate dehydrogenase, formate dehydrogenase N, FDH-N, nitrate inducible Fdn, nitrate inducible formate dehydrogenase

Summary:
This is the first step in the metabolism of formate under anaerobic conditions.

Enzyme Commission Summary:
The enzyme contains molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters and two heme b groups. Formate dehydrogenase-N oxidizes formate in the periplasm, transferring electrons via the menaquinone pool in the cytoplasmic membrane to a dissimilatory nitrate reductase (EC 1.7.5.1), which transfers electrons to nitrate in the cytoplasm. The system generates proton motive force under anaerobic conditions [Jormakka02].

Citations: [Enoch75, Jormakka02a]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.1.5.6 , ENZYME:EC:1.1.5.6 , IUBMB-ExplorEnz:EC:1.1.5.6


References

Enoch75: Enoch HG, Lester RL (1975). "The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli." J Biol Chem 1975;250(17);6693-705. PMID: 1099093

Jormakka02: Jormakka M, Tornroth S, Abramson J, Byrne B, Iwata S (2002). "Purification and crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli." Acta Crystallogr D Biol Crystallogr 58(Pt 1);160-2. PMID: 11752799

Jormakka02a: Jormakka M, Tornroth S, Byrne B, Iwata S (2002). "Molecular basis of proton motive force generation: structure of formate dehydrogenase-N." Science 295(5561);1863-8. PMID: 11884747


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 Thu Nov 27, 2014, BIOCYC14B.