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Literature summary for 1.2.1.12 extracted from

  • Copeland, L.; Zammit, A.
    Kinetic properties of NAD-dependent glyceraldehyde-3-phosphate dehydrogenase from the host fraction of soybean root nodules (1994), Arch. Biochem. Biophys., 312, 107-113.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2,3-diphosphoglycerate
-
Glycine max
AMP
-
Glycine max
NADH competitive with respect to NAD+ and phosphate Glycine max

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Glycine max

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Glycine max
-
-
-

Reaction

Reaction Comment Organism Reaction ID
D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+ bi-uni-uni-uni-ping-pong mechanism in which NAD+ and phosphate interact sequentially with the enzyme, followed in turn by the release of 3-phospho-D-glyceroyl phosphate, the addition of D-glyceraldehyde-3-phosphate, and the release of NADH. At pH 7.2, NAD+ binds to the enzyme in a rapid-equilibrium fashion, whereas at pH 8.8 there is rapid-equilibrium addition of both NAD+ and phosphate to the enzyme Glycine max

Source Tissue

Source Tissue Comment Organism Textmining
nodule
-
Glycine max
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Glycine max 3-phospho-D-glyceroyl phosphate + NADH
-
?

pH Stability

pH Stability pH Stability Maximum Comment Organism
8
-
very labile, especially above pH 8.0 Glycine max

Cofactor

Cofactor Comment Organism Structure
NAD+ at pH 8.8 there is rapid-equilibrium addition of both NAD+ and phosphate to the enzyme Glycine max