Literature summary 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.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.2.1.12	-	Geobacillus stearothermophilus

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.2.1.12	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

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	D-glyceraldehyde 3-phosphate + phosphate + NAD+	-	Geobacillus stearothermophilus	3-phospho-D-glyceroyl phosphate + NADH	-	?

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
1.2.1.12	additional information	-	three salt bridges made by each subunit to others would make a major contribution to thermostability of the tetramer	Geobacillus stearothermophilus
1.2.1.12	60	70	retains structural integrity and enzymatic activity up to	Geobacillus stearothermophilus

Cofactor

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

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Release 2023.1 (January 2023)