Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
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 / EGO
Search PMC articles PubMed articles NCBI proteins

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⁺ $\rightleftharpoons$ 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

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

• Caputto R and Dixon M. "Crystallization and identity of the triose and triosephosphate dehydrogenase of muscle". N (Lond.). Nature: 630–631.
• Cori GT, Slein MW and Cori CF (1948). "Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle". J. Biol. Chem. 173: 605–618.
• Hageman RH and 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 and Christian W (1939). "Isolierung und Krystallisation des Proteins des oxydierenden Garungsferments". Biochem. Z. 303: 40–68.
• Warburg O and Christian W (1939). "Isolierung und Krystallisation des Proteins des oxydierenden Garungsferments". Biochem. Z. 303: 40–68.