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Literature summary for 1.2.1.12 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

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-
Thermotoga maritima
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Oryctolagus cuniculus 3-phospho-D-glyceroyl phosphate + NADH + H+
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Thermotoga maritima 3-phospho-D-glyceroyl phosphate + NADH + H+
-
?

Synonyms

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
66
-
melting temperature at 66°C Oryctolagus cuniculus
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

Cofactor Comment Organism Structure
NAD+
-
Oryctolagus cuniculus
NAD+
-
Thermotoga maritima