General Stability | Organism |
---|---|
alpha-crystallin accelerates the thermal inactivation of GAPDH, while GroEL does not affect thermal inactivation and denaturation of GAPDH | Oryctolagus cuniculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
skeletal muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Oryctolagus cuniculus | 3-phospho-D-glyceroyl phosphate + NADH | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | - |
Oryctolagus cuniculus |
Synonyms | Comment | Organism |
---|---|---|
GAPDH | - |
Oryctolagus cuniculus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
GAPDH is inactivated at 45°C, alpha-crystallin accelerates the thermal inactivation of GAPDH at 45°C and reduces thermostability of the enzyme, while GroEL does not affect thermal inactivation and denaturation of GAPDH | Oryctolagus cuniculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Oryctolagus cuniculus |