Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

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glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
3gpd.jpg
Identifiers
EC number 1.2.1.12
CAS number 9001-50-7
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

In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) is an enzyme that catalyzes the chemical reaction

D-glyceraldehyde 3-phosphate + phosphate + NAD+ 3-phospho-D-glyceroyl phosphate + NADH + H+

The 3 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, and NAD+, whereas its 3 products are 3-phospho-D-glyceroyl phosphate, NADH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating). Other names in common use include triosephosphate dehydrogenase, dehydrogenase, glyceraldehyde phosphate, phosphoglyceraldehyde dehydrogenase, 3-phosphoglyceraldehyde dehydrogenase, NAD+-dependent glyceraldehyde phosphate dehydrogenase, glyceraldehyde phosphate dehydrogenase (NAD+), glyceraldehyde-3-phosphate dehydrogenase (NAD+), NADH-glyceraldehyde phosphate dehydrogenase, and glyceraldehyde-3-P-dehydrogenase. This enzyme participates in glycolysis / gluconeogenesis.

Structural studies[edit]

As of late 2007, 49 structures have been solved for this class of enzymes, with PDB accession codes 1A7K, 1B7G, 1CER, 1CF2, 1CRW, 1DBV, 1DC3, 1DC4, 1DC5, 1DC6, 1DSS, 1GAD, 1GAE, 1GD1, 1GGA, 1GPD, 1GYP, 1GYQ, 1HDG, 1I32, 1I33, 1IHX, 1IHY, 1J0X, 1K3T, 1ML3, 1NPT, 1NQ5, 1NQA, 1NQO, 1OBF, 1QXS, 1S7C, 1SZJ, 1U8F, 1VC2, 1YWG, 1ZNQ, 2B4R, 2B4T, 2DBV, 2EP7, 2G82, 2GD1, 2I5P, 3DBV, 3GPD, 4DBV, and 4GPD.

References[edit]

  • Caputto R; Dixon M. "Crystallization and identity of the triose and triosephosphate dehydrogenase of muscle". N. Lond. Nature: 630–631. 
  • Cori GT; Slein MW (1948). "Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle". J. Biol. Chem. 173: 605–618. 
  • Hageman RH; Arnon DI (1955). "The isolation of triosephosphate dehydrogenase from pea seeds". Arch. Biochem. Biophys. 55 (1): 162–168. doi:10.1016/0003-9861(55)90554-3. PMID 14362612. 
  • Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 243-273.
  • Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 243-273.
  • Warburg O; Christian W (1939). "Isolierung und Krystallisation des Proteins des oxydierenden Garungsferments". Biochem. Z. 303: 40–68. 
  • Warburg O; Christian W (1939). "Isolierung und Krystallisation des Proteins des oxydierenden Garungsferments". Biochem. Z. 303: 40–68.