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Literature summary extracted from

  • Corbier, C.; Clermont, S.; Billard, P.; Skarzynski, T.; Branlant, C.; Wonacott, A.; Branlant, G.
    Probing the coenzyme specificity of glyceraldehyde-3-phosphate dehydrogenases by site-directed mutagenesis (1990), Biochemistry, 29, 7101-7106.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.12
-
 Geobacillus stearothermophilus

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.12 L187A/P188S the mutant is catalytically active not only with NAD+, as the wild-type enzyme, but also with NADP+ Geobacillus stearothermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.12 3-(chloroacetyl)-pyridine adenine dinculeotide
-
 Geobacillus stearothermophilus
1.2.1.12 NAD+ competitive against NADH Geobacillus stearothermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.12 additional information
-
 additional information
-
 Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.12 Geobacillus stearothermophilus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.12 3-phospho-D-glyceroyl phosphate + NADH
-
 Geobacillus stearothermophilus D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 r
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Geobacillus stearothermophilus 3-phospho-D-glyceroyl phosphate + NADH
-
 r
1.2.1.12 additional information mutant enzyme L187A/P188S is catalytically active not only with NAD+, as the wild-type enzyme, but also with NADP+ Geobacillus stearothermophilus ?
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.12 NAD+
-
 Geobacillus stearothermophilus
1.2.1.12 NADH cofactor Geobacillus stearothermophilus