Glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)

Last updated
glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
Identifiers
EC no. 1.2.7.6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) (EC 1.2.7.6) is an enzyme that catalyzes the chemical reaction

+ 2 oxidised ferredoxin
 
 
H2O
2 H+
Glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
H2O
2 H+
 
+ 2 reduced ferredoxin
 

The three substrates of this enzyme are D-glyceraldehyde-3-phosphate, oxidized ferredoxin, and water. Its products are 3-phospho-D-glyceric acid, reduced ferredoxin and two protons. [1] [2] [3]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase. Other names in common use include GAPOR, glyceraldehyde-3-phosphate Fd oxidoreductase, and glyceraldehyde-3-phosphate ferredoxin reductase.

References

  1. Enzyme 1.2.7.6 at KEGG Pathway Database.
  2. Mukund S, Adams MW (1995). "Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus". J. Biol. Chem. 270 (15): 8389–92. doi: 10.1074/jbc.270.15.8389 . PMID   7721730.
  3. Roy R, Menon AL, Adams MW (2001). "Aldehyde Oxidoreductases from Pyrococcus furiosus". Hyperthermophilic enzymes Part B. Methods in Enzymology. Vol. 331. pp. 132–44. doi:10.1016/S0076-6879(01)31052-2. ISBN   978-0-12-182232-3. PMID   11265456.