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Literature summary for 1.2.1.12 extracted from

  • Biesecker, G.; Harris, J.I.; Thierry, J.C.; Walker, J.E.; Wonacott, A.J.
    Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus (1977), Nature, 266, 328-333.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Geobacillus stearothermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
the enzyme possesses precise 222 symmetry. Pairs of active sites are linked through a flexible polypeptide loop which probably mediates the structural changes giving rise to cooperative effects. Three additional salt bridges made by each subunit to others would make a major contribution to thermostability of the tetramer Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Substrates and Products (Substrate)

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
three salt bridges made by each subunit to others would make a major contribution to thermostability of the tetramer Geobacillus stearothermophilus
60 70 retains structural integrity and enzymatic activity up to Geobacillus stearothermophilus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Geobacillus stearothermophilus