Biology:Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

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glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
3gpd.jpg
Identifiers
EC number1.2.1.12
CAS number9001-50-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / 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+ [math]\displaystyle{ \rightleftharpoons }[/math] 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 participates in glycolysis / gluconeogenesis.

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.

References

Further reading

  • "Crystallization and identity of the triose and triosephosphate dehydrogenases of muscle". Nature 156 (3969): 630–631. 1945. doi:10.1038/156630c0. PMID 21006487. Bibcode1945Natur.156..630.. 
  • Cori GT; Slein MW (1948). "Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle". J. Biol. Chem. 173 (2): 605–618. PMID 18910716. 
  • "The isolation of triosephosphate dehydrogenase from pea seeds". Archives of Biochemistry and Biophysics 55 (1): 162–8. March 1955. doi:10.1016/0003-9861(55)90554-3. PMID 14362612. 
  • The Enzymes. 7 (2nd ed.). New York: Academic Press. 1963. pp. 243–273. 
  • "Isolierung und Krystallisation des Proteins des oxydierenden Garungsferments". Biochem. Z. 303: 40–68. 1939.