Activating Compound | Comment | Organism | Structure |
---|---|---|---|
C1-tetrahydrofolate synthase | 10-formyltetrahydrofolate synthetase activity of trifunctional enzyme causes together with its substrates MgATP, formate, and tetrahydrofolate an 3fold increase of initial velocity | Oryctolagus cuniculus | |
NADPH | activates | Oryctolagus cuniculus | |
serine hydroxymethyltransferase | addition of SHMT and of its substrate L-serine increases the initial reaction rate by 1.8fold with 10-formyltetrahydropteroylpentaglutamate as substrate, SHMT increases the release of product | Oryctolagus cuniculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
tetrahydrofolate | potent, competitive product inhibitor | Oryctolagus cuniculus | |
Tetrahydropteroylpentaglutamate | strong product inhibition | Oryctolagus cuniculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Oryctolagus cuniculus | 5829 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
10-formyltetrahydrofolate + NADP+ + H2O | Oryctolagus cuniculus | - |
tetrahydrofolate + CO2 + NADPH + H+ | - |
ir | |
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O | Oryctolagus cuniculus | important site of binding of folylpolyglutamates in liver, regulation of the interconversion of 10-formyltetrahydropteroylpolyglutamate to tetrahydropteroylpolyglutamate and therefore of the high-energy formyl charge of the cell | tetrahydropteroylpentaglutamate + CO2 + NADPH | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | very high concentrations, two livers, 120 g, contain about 360 mg enzyme | Oryctolagus cuniculus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Oryctolagus cuniculus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
10-formyl-5,8-dideazafolate + NADP+ + H2O | good substrate | Oryctolagus cuniculus | 5,8-dideazafolate + CO2 + NADPH + H+ | - |
ir | |
10-formyl-5,8-dideazafolate tetraglutamate + NADP+ + H2O | - |
Oryctolagus cuniculus | 5,8-dideazafolate tetraglutamate + CO2 + NADPH + H+ | tightly bound product | ir | |
10-formyltetrahydrofolate + NADP+ + H2O | - |
Oryctolagus cuniculus | tetrahydrofolate + CO2 + NADPH + H+ | - |
ir | |
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O | product binds 60fold more tightly than the substrate | Oryctolagus cuniculus | tetrahydropteroylpentaglutamate + CO2 + NADPH | - |
ir | |
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O | important site of binding of folylpolyglutamates in liver, regulation of the interconversion of 10-formyltetrahydropteroylpolyglutamate to tetrahydropteroylpolyglutamate and therefore of the high-energy formyl charge of the cell | Oryctolagus cuniculus | tetrahydropteroylpentaglutamate + CO2 + NADPH | - |
ir | |
10-formyltetrahydropteroylpolyglutamate + NADP+ + H2O | - |
Oryctolagus cuniculus | tetrahydropteroylpolyglutamate + CO2 + NADPH + H+ | - |
ir |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Oryctolagus cuniculus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.867 | - |
10-formyltetrahydropteroylpentaglutamate | with excess substrate, reaction cycle in combination with C1-tetrahydrofolate synthase, lower value than for dehydrogenase alone | Oryctolagus cuniculus | |
0.9 | - |
10-formyltetrahydropteroylpentaglutamate | at 30°C | Oryctolagus cuniculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
10-formyltetrahydrofolate | 10-formyltetrahydrofolate | Oryctolagus cuniculus | |
10-formyltetrahydrofolate | pentaglutamate form as coenzyme is very tightly bound to enzyme | Oryctolagus cuniculus | |
folate | 10-formyl-5,8-dideazafolate and 5,8-dideazafolate | Oryctolagus cuniculus | |
NADP+ | - |
Oryctolagus cuniculus | |
tetrahydrofolate | - |
Oryctolagus cuniculus |