EC Number | General Stability | Organism |
---|---|---|
6.3.4.3 | the binding of tetrahydropteroylpolyglutamate, MgATP2-, and NH4+ alters the susceptibility to digestion by chymotrypsin | Oryctolagus cuniculus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.4.3 | additional information | - |
additional information | effect of polyglutamate chain length of tetrahydropteroyl-(Glu)n on the Km values of formate and MgATP2- | Oryctolagus cuniculus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.3.4.3 | Oryctolagus cuniculus | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
6.3.4.3 | liver | - |
Oryctolagus cuniculus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.4.3 | ATP + formate + tetrahydrofolate | - |
Oryctolagus cuniculus | ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
6.3.4.3 | ATP + formate + tetrahydropteroyl-(Glu)n | n: 1-5 | Oryctolagus cuniculus | ADP + phosphate + 10-formyltetrahydropteroyl-(Glu)n | - |
? |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.3.4.3 | additional information | - |
the binding of tetrahydropteroylpolyglutamate, MgATP2-, and NH4+ increases the denaturation temperature by 12°C and abolishes the cold lability of the enzyme | Oryctolagus cuniculus |