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Literature summary extracted from

  • Harmony, J.A.K.; Shaffer, P.J.; Himes, R.H.
    Cation- and anion-dependent reassociation of formyltetrahydrofolate synthetase subunits (1974), J. Biol. Chem., 249, 394-401.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.4.3 spermine stimulates activity only in absence of NH4+ Clostridium cylindrosporum

General Stability

EC Number General Stability Organism
6.3.4.3 addition of monovalent cations to the dissociated enzyme causes the inactive monomers to reassociate to the active tetramer. The order of cation effectiveness is NH4+ > Tl+ > Rb+ ~ K+ > Cs+ > Na+ ~ Li+. The rate and extent of reactivation is influenced by the counter ion: sulfate and phosphate stimulate reassociation, thiocyanate, trichloroacetate, and perchlorate completly inhibit reassociation. The extent of reactivation is dependent upon protein concentration. The optimum protein concentration depends on the pH at which reactivation is performed Clostridium cylindrosporum

Organism

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

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
6.3.4.3 tetramer enzymes exist as a catalytically active tetramer in the presence of specific monovalent cations or as an inactive monomer in their absence Clostridium cylindrosporum
6.3.4.3 tetramer enzymes exist as a catalytically active tetramer in the presence of specific monovalent cations or as an inactive monomer in their absence Clostridium acidi-urici