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
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 1.8.7.2

Superclasses: 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: 1.8.7.2

Enzymes and Genes:
ferredoxin-thioredoxin reductase Inferred from experiment : ftrV , ftrC ( Synechocystis sp. PCC 6803 )

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: ferredoxin:thioredoxin reductase

Enzyme Commission Synonyms: ferredoxin:thioredoxin disulfide oxidoreductase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -9.900482 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Contains a [4Fe-4S] cluster and internal disulfide. It forms a mixed disulfide with thioredoxin on one side, and docks ferredoxin on the other side, enabling two one-electron transfers. The reduced thioredoxins generated by the enzyme activate the Calvin cycle enzymes EC 3.1.3.11 (fructose-1,6-bisphosphatase), EC 3.1.3.37 (sedoheptulose-bisphosphatase) and EC 2.7.1.19 (phosphoribulokinase) as well as other chloroplast enzymes by disulfide reduction.

Citations: [Buchanan91, Chow95, Staples96]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.8.7.2 , ENZYME:EC:1.8.7.2 , IUBMB-ExplorEnz:EC:1.8.7.2

Credits:
Revised 16-Mar-2010 by Caspi R , SRI International


References

Buchanan91: Buchanan BB (1991). "Regulation of CO2 assimilation in oxygenic photosynthesis: the ferredoxin/thioredoxin system. Perspective on its discovery, present status, and future development." Arch Biochem Biophys 288(1);1-9. PMID: 1910303

Chow95: Chow LP, Iwadate H, Yano K, Kamo M, Tsugita A, Gardet-Salvi L, Stritt-Etter AL, Schurmann P (1995). "Amino acid sequence of spinach ferredoxin:thioredoxin reductase catalytic subunit and identification of thiol groups constituting a redox-active disulfide and a [4Fe-4S] cluster." Eur J Biochem 231(1);149-56. PMID: 7628465

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

Staples96: Staples CR, Ameyibor E, Fu W, Gardet-Salvi L, Stritt-Etter AL, Schurmann P, Knaff DB, Johnson MK (1996). "The function and properties of the iron-sulfur center in spinach ferredoxin: thioredoxin reductase: a new biological role for iron-sulfur clusters." Biochemistry 35(35);11425-34. PMID: 8784198


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 Mon Nov 24, 2014, BIOCYC14A.