Literature summary for 6.3.4.3 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.

Activating Compound

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

General Stability

General Stability	Organism
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

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

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

Substrates and Products (Substrate)

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	-	?

Subunits

Subunits	Comment	Organism
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
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