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Literature summary for 6.3.4.3 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

Organism UniProt Comment Textmining
Clostridium acidi-urici
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-
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Clostridium cylindrosporum
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-
-

Renatured (Commentary)

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 and Products (Substrate)

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