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Literature summary extracted from

  • Hajdu, I.; Bothe, C.; Szilagyi, A.; Kardos, J.; Gal, P.; Zavodszky, P.
    Adjustment of conformational flexibility of glyceraldehyde-3-phosphate dehydrogenase as a means of thermal adaptation and allosteric regulation (2008), Eur. Biophys. J., 37, 1139-1144.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.12 Oryctolagus cuniculus
-
-
-
1.2.1.12 Thermotoga maritima
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.12 muscle
-
 Oryctolagus cuniculus
-

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+
-
 Oryctolagus cuniculus 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Thermotoga maritima 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.12 D-glyceraldehyde-3-phosphate dehydrogenase
-
 Thermotoga maritima
1.2.1.12 GAPDH
-
 Oryctolagus cuniculus
1.2.1.12 GAPDH
-
 Thermotoga maritima

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.2.1.12 66
-
 melting temperature at 66°C Oryctolagus cuniculus
1.2.1.12 80 102 the enzyme is fully active at temperatures near 80°C but has very low activity at room temperature, the melting temperature is at 102°C Thermotoga maritima

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.12 NAD+
-
 Oryctolagus cuniculus
1.2.1.12 NAD+
-
 Thermotoga maritima