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Literature summary extracted from

  • Garrison, C.K.; Harmony, J.A.K.; Himes, R.H.
    Renaturation of formyltetrahydrofolate synthetase from urea and guanidinium chloride solution (1976), Biochim. Biophys. Acta, 446, 301-309.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.3 Clostridium acidi-urici
-
-
-
6.3.4.3 Clostridium cylindrosporum
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
6.3.4.3 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
6.3.4.3 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.3 ATP + formate + tetrahydrofolate
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Clostridium cylindrosporum ADP + phosphate + 10-formyltetrahydrofolate
-
?
6.3.4.3 ATP + formate + tetrahydrofolate
-
Clostridium acidi-urici ADP + phosphate + 10-formyltetrahydrofolate
-
?