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MetaCyc Reaction: 1.20.2.1

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Composite Reactions Electron-Transfer-Reactions
Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 1.20.2.1

Enzymes and Genes:
arsenite oxidoreductase Inferred from experiment ( arsenite-oxidizing bacterium NT-14 )

In Pathway: arsenite oxidation I (respiratory)

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: arsenate reductase (cytochrome c)

Enzyme Commission Synonyms: arsenite oxidase (ambiguous)

Standard Gibbs Free Energy (ΔrG in kcal/mol): -0.25228882 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
A molybdoprotein containing iron-sulfur clusters. Isolated from α-proteobacteria. Unlike EC 1.20.9.1, arsenate reductase (azurin), it does not use azurin as acceptor.

Citations: [vandenHoven04, Santini07, Branco09, Lieutaud10]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.20.2.1 , ENZYME:EC:1.20.2.1 , IUBMB-ExplorEnz:EC:1.20.2.1

Credits:
Created 24-Aug-2011 by Caspi R , SRI International


References

Branco09: Branco R, Francisco R, Chung AP, Morais PV (2009). "Identification of an aox system that requires cytochrome c in the highly arsenic-resistant bacterium Ochrobactrum tritici SCII24." Appl Environ Microbiol 75(15);5141-7. PMID: 19525272

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Lieutaud10: Lieutaud A, van Lis R, Duval S, Capowiez L, Muller D, Lebrun R, Lignon S, Fardeau ML, Lett MC, Nitschke W, Schoepp-Cothenet B (2010). "Arsenite oxidase from Ralstonia sp. 22: characterization of the enzyme and its interaction with soluble cytochromes." J Biol Chem 285(27);20433-41. PMID: 20421652

Santini07: Santini JM, Kappler U, Ward SA, Honeychurch MJ, vanden Hoven RN, Bernhardt PV (2007). "The NT-26 cytochrome c552 and its role in arsenite oxidation." Biochim Biophys Acta 1767(2);189-96. PMID: 17306216

vandenHoven04: vanden Hoven RN, Santini JM (2004). "Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: the arsenite oxidase and its physiological electron acceptor." Biochim Biophys Acta 1656(2-3);148-55. PMID: 15178476


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Feb 28, 2015, biocyc12.