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Literature summary for 1.2.1.12 extracted from

  • Roitel, O.; Sergienko, E.; Branlant, G.
    Dimers generated from tetrameric phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus are inactive but exhibit cooperativity in NAD binding (1999), Biochemistry, 38, 16084-16091.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D186G behavior in NAD+ binding is similar to that of the wild type enzyme Geobacillus stearothermophilus
D186G/E276G positive cooperativity in binding the coenzyme NAD+ Geobacillus stearothermophilus
E276G behavior in NAD+ binding is similar to that of the wild type enzyme Geobacillus stearothermophilus
Y46G behavior in NAD+ binding is similar to that of the wild type enzyme Geobacillus stearothermophilus
Y46G/S48G positive cooperativity in binding the coenzyme NAD+ Geobacillus stearothermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
NAD+ mutant enzyme S48G Geobacillus stearothermophilus
0.05
-
NAD+ wild-type enzyme Geobacillus stearothermophilus
0.07
-
NAD+ mutant enzyme E276G Geobacillus stearothermophilus
0.33
-
NAD+ mutant enzyme S186G Geobacillus stearothermophilus
0.8
-
D-glyceraldehyde 3-phosphate mutant enzyme Y46G Geobacillus stearothermophilus
0.9
-
D-glyceraldehyde 3-phosphate mutant enzyme E276G Geobacillus stearothermophilus
1
-
D-glyceraldehyde 3-phosphate mutant enzyme D186G and mutant enzyme S48G Geobacillus stearothermophilus
1.1
-
D-glyceraldehyde 3-phosphate wild-type enzyme Geobacillus stearothermophilus
7
-
phosphate mutant enzyme E276G and mutant enzyme S48G Geobacillus stearothermophilus
8
-
phosphate mutant enzyme Y46G Geobacillus stearothermophilus
18
-
phosphate mutant enzyme D186G Geobacillus stearothermophilus
37
-
phosphate wild-type enzyme Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus P00362
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More dimers generated from the tetrameric enzyme are inactive but exhibit cooperativity in NAD+ binding Geobacillus stearothermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information
-
Geobacillus stearothermophilus

Cofactor

Cofactor Comment Organism Structure
NAD+ dimers generated from the tetrameric enzyme are inactive but exhibit cooperativity in NAD+ binding Geobacillus stearothermophilus