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Literature summary for 1.2.1.12 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)

Crystallization (Comment) Organism
-
Geobacillus stearothermophilus

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-phospho-D-glyceroyl phosphate + NADH
-
Geobacillus stearothermophilus D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Geobacillus stearothermophilus 3-phospho-D-glyceroyl phosphate + NADH
-
r
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

Cofactor Comment Organism Structure
NAD+
-
Geobacillus stearothermophilus
NADH cofactor Geobacillus stearothermophilus