Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium acidi-urici | - |
- |
- |
Clostridium cylindrosporum | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
enzymes denatured in 6 M urea and 4 M guanidinium chloride refold upon dilution of the denaturant-protein solution to give final concentrations of 0.5 M urea or 0.1 M guanidinium chloride. In presence of NH4+, but not in its absence the refolded proteins associate to produce the catalytically active tetramer. 80% of the enzymatic acitivity is recovered | Clostridium cylindrosporum |
enzymes denatured in 6 M urea and 4 M guanidinium chloride refold upon dilution of the denaturant-protein solution to give final concentrations of 0.5 M urea or 0.1 M guanidinium chloride. In presence of NH4+, but not in its absence the refolded proteins associate to produce the catalytically active tetramer. 80% of the enzymatic acitivity is recovered | Clostridium acidi-urici |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + formate + tetrahydrofolate | - |
Clostridium cylindrosporum | ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
ATP + formate + tetrahydrofolate | - |
Clostridium acidi-urici | ADP + phosphate + 10-formyltetrahydrofolate | - |
? |