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Literature summary extracted from

  • Villar, E.; Schuster, B.; Peterson, D.; Schirch, V.
    C1-Tetrahydrofolate synthase from rabbit liver. Structural and kinetic properties of the enzyme and its two domains (1985), J. Biol. Chem., 260, 2245-2252.
    View publication on PubMed

General Stability

EC Number General Stability Organism
6.3.4.3 K+ or NH4+ increase stability of the large domain of the multifuncional enzyme, that contains the active site for the 10-formyltetrahydrofolate synthetase Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.5 0.002
-
 5,10-methylenetetrahydrofolate
-
 Oryctolagus cuniculus
1.5.1.5 0.004
-
 NADP+
-
 Oryctolagus cuniculus
6.3.4.3 0.067
-
 ATP
-
 Oryctolagus cuniculus
6.3.4.3 0.166
-
 formate
-
 Oryctolagus cuniculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.4.3 K+ Km: 4 mM Oryctolagus cuniculus
6.3.4.3 K+ K+ or NH4+ required Oryctolagus cuniculus
6.3.4.3 NH4+ Km: 1.8 mM Oryctolagus cuniculus
6.3.4.3 NH4+ K+ or NH4+ required Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.5 5,10-methylenetetrahydrofolate + NADP+ Oryctolagus cuniculus
-
 5,10-methenyltetrahydrofolate + NADPH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.5 Oryctolagus cuniculus
-
-
-
6.3.4.3 Oryctolagus cuniculus
-
 trifunctional enzyme with 10-formyltetrahydrofolate synthetase, EC 6.3.4.3, 5,10-methenyltetrahydrofolate cyclohydrolase, EC 3.5.4.9, and 5,10-methylenetetrahydrofolate dehydrogenase activity, EC 1.5.1.5
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.5 trifunctional enzyme: methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrase, formyltetrahydrofolate synthetase Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.5 liver
-
 Oryctolagus cuniculus
-
6.3.4.3 liver
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.5 5,10-methylenetetrahydrofolate + NADP+
-
 Oryctolagus cuniculus 5,10-methenyltetrahydrofolate + NADPH + H+
-
 ?
6.3.4.3 ATP + formate + tetrahydrofolate ATP in form of MgATP2- Oryctolagus cuniculus ADP + phosphate + 10-formyltetrahydrofolate
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.4.3 More a tryptic fragment that contains 10-formyltetrahydrofolate synthetase activity is a dimer, MW 66000 Oryctolagus cuniculus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
6.3.4.3 23
-
 the large domain of the multifuncional enzyme, that contains the active site for the 10-formyltetrahydrofolate synthetase is more stable at 23°C than at 0°C Oryctolagus cuniculus
6.3.4.3 47
-
 transition at 47°C is due to the denaturation of a domain which binds MgATP2- and contains the synthetase active site Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.5 NADP+
-
 Oryctolagus cuniculus