Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
Identifiers
EC no.	1.2.1.12
CAS no.	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
Search PMC articles PubMed articles NCBI proteins

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

D-glyceraldehyde-3-phosphate

+ NAD⁺

 

 

P_i

H⁺

P_i

H⁺

 

1,3-bisphosphoglyceric acid

+ NADH

 

The three substrates of this enzyme are D-glyceraldehyde-3-phosphate, phosphate (P_i), and oxidised nicotinamide adenine dinucleotide (NAD⁺). Its products are 1,3-bisphosphoglyceric acid, reduced NADH, and a proton. ^[1] This enzyme participates in glycolysis and gluconeogenesis. ^{[2] [3] [4]}

Nomenclature

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.

See also

• Glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) which catalyses the same reaction using nicotinamide adenine dinucleotide phosphate as its cofactor

References

1. Enzyme 1.2.1.12 at KEGG Pathway Database.
2. Caputto R, Dixon M (1945). "Crystallization and identity of the triose and triosephosphate dehydrogenases of muscle". Nature. 156 (3969): 630–631. Bibcode:1945Natur.156..630.. doi:10.1038/156630c0. PMID   21006487. S2CID   4104880.
3. Cori GT; Slein MW (1948). "Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle". J. Biol. Chem. 173 (2): 605–618. doi: 10.1016/S0021-9258(18)57432-9 . PMID   18910716.
4. Hageman RH, Arnon DI (March 1955). "The isolation of triosephosphate dehydrogenase from pea seeds". Archives of Biochemistry and Biophysics. 55 (1): 162–8. doi:10.1016/0003-9861(55)90554-3. PMID   14362612.

Further reading

• Boyer PD, Lardy H, Myrback K, eds. (1963). The Enzymes. Vol. 7 (2nd ed.). New York: Academic Press. pp. 243–273.
• Warburg O, Christian W (1939). "Isolierung und Krystallisation des Proteins des oxydierenden Garungsferments". Biochem. Z. 303: 40–68.