EC 1.2.1.12 - Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

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IntEnz Enzyme Nomenclature
EC 1.2.1.12

Names

Accepted name:
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
Other names:
3-phosphoglyceraldehyde dehydrogenase
NAD-dependent glyceraldehyde phosphate dehydrogenase
NADH-glyceraldehyde phosphate dehydrogenase
dehydrogenase, glyceraldehyde phosphate
glyceraldehyde phosphate dehydrogenase (NAD)
glyceraldehyde-3-P-dehydrogenase
glyceraldehyde-3-phosphate dehydrogenase (NAD)
phosphoglyceraldehyde dehydrogenase
triosephosphate dehydrogenase
Systematic name:
D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating)

Reaction

Comments:

Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00069
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004365
CAS Registry Number: 9001-50-7
UniProtKB/Swiss-Prot: (256) [show] [UniProt]

References

  1. Caputto, R. and Dixon, M.
    Crystallization and identity of the triose and triosephosphate dehydrogenase of muscle.
    Nature (Lond.) 156: 630-631 (1945).
  2. Cori, G.T., Slein, M.W. and Cori, C.F.
    Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle.
    J. Biol. Chem. 173: 605-618 (1948).
  3. Hageman, R.H. and Arnon, D.I.
    The isolation of triosephosphate dehydrogenase from pea seeds.
    Arch. Biochem. Biophys. 55: 162-168 (1955).
  4. Velick, S.F. and Furfine, C.
    Glyceraldehyde 3-phosphate dehydrogenase.
    In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes, 2nd ed. vol. 7, Academic Press, New York, 1963, 243-273
  5. Warburg, O. and Christian, W.
    Isolierung und Krystallisation des Proteins des oxydierenden Gärungsferments.
    Biochem. Z. 303: 40-68 (1939).

[EC 1.2.1.12 created 1961]