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Literature summary for 6.3.4.3 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
Search for more literature for 6.3.4.3

General Stability

General Stability Organism
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.067
-
 ATP
-
 Oryctolagus cuniculus
0.166
-
 formate
-
 Oryctolagus cuniculus

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
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
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + formate + tetrahydrofolate ATP in form of MgATP2- Oryctolagus cuniculus ADP + phosphate + 10-formyltetrahydrofolate
-
 ?

Subunits

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
47
-
 transition at 47°C is due to the denaturation of a domain which binds MgATP2- and contains the synthetase active site Oryctolagus cuniculus