EC 1.8.7.2 - Ferredoxin:thioredoxin reductase

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IntEnz Enzyme Nomenclature
EC 1.8.7.2

Names

Accepted name:
ferredoxin:thioredoxin reductase
Systematic name:
ferredoxin:thioredoxin disulfide oxidoreductase

Reaction

Cofactor

Comments:

The enzyme 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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0103012
UniProtKB/Swiss-Prot: (11) [show] [UniProt]

References

  1. Buchanan, B. B.
    Regulation of CO2 assimilation in oxygenic photosynthesis: the ferredoxin/thioredoxin system. Perspective on its discovery, present status, and future development.
    Arch. Biochem. Biophys. 288: 1-9 (1991). [PMID: 1910303]
  2. Chow, L. P., Iwadate, H., Yano, K., Kamo, M., Tsugita, A., Gardet-Salvi, L., Stritt-Etter, A. L., Schurmann, P.
    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: 149-156 (1995). [PMID: 7628465]
  3. Staples, C. R., Ameyibor, E., Fu, W., Gardet-Salvi, L., Stritt-Etter, A. L., Schurmann, P., Knaff, D. B., Johnson, M. K.
    The function and properties of the iron-sulfur center in spinach ferredoxin: thioredoxin reductase: a new biological role for iron-sulfur clusters.
    Biochemistry 35: 11425-11434 (1996). [PMID: 8784198]

[EC 1.8.7.2 created 2010]