Metabolic Modeling Tutorial
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BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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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 Sat Dec 20, 2014, biocyc13.