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Literature summary extracted from

  • Kim, D.W.; Huang, T.; Schirch, D.; Schirch, V.
    Properties of tetrahydropteroylpentaglutamate bound to 10-formyltetrahydrofolate dehydrogenase (1996), Biochemistry, 35, 15772-15783.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.5.1.6 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
1.5.1.6 NADPH activates Oryctolagus cuniculus
1.5.1.6 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

EC Number Inhibitors Comment Organism Structure
1.5.1.6 tetrahydrofolate potent, competitive product inhibitor Oryctolagus cuniculus
1.5.1.6 Tetrahydropteroylpentaglutamate strong product inhibition Oryctolagus cuniculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.5.1.6 cytosol
-
 Oryctolagus cuniculus 5829
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O Oryctolagus cuniculus
-
 tetrahydrofolate + CO2 + NADPH + H+
-
 ir
1.5.1.6 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

EC Number Organism UniProt Comment Textmining
1.5.1.6 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.6
-
 Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.6 liver very high concentrations, two livers, 120 g, contain about 360 mg enzyme Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.6 additional information
-
-
 Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.6 10-formyl-5,8-dideazafolate + NADP+ + H2O good substrate Oryctolagus cuniculus 5,8-dideazafolate + CO2 + NADPH + H+
-
 ir
1.5.1.6 10-formyl-5,8-dideazafolate tetraglutamate + NADP+ + H2O
-
 Oryctolagus cuniculus 5,8-dideazafolate tetraglutamate + CO2 + NADPH + H+ tightly bound product ir
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O
-
 Oryctolagus cuniculus tetrahydrofolate + CO2 + NADPH + H+
-
 ir
1.5.1.6 10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O product binds 60fold more tightly than the substrate Oryctolagus cuniculus tetrahydropteroylpentaglutamate + CO2 + NADPH
-
 ir
1.5.1.6 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
1.5.1.6 10-formyltetrahydropteroylpolyglutamate + NADP+ + H2O
-
 Oryctolagus cuniculus tetrahydropteroylpolyglutamate + CO2 + NADPH + H+
-
 ir

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.6 30
-
 assay at Oryctolagus cuniculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.6 0.867
-
 10-formyltetrahydropteroylpentaglutamate with excess substrate, reaction cycle in combination with C1-tetrahydrofolate synthase, lower value than for dehydrogenase alone Oryctolagus cuniculus
1.5.1.6 0.9
-
 10-formyltetrahydropteroylpentaglutamate at 30°C Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.6 10-formyltetrahydrofolate 10-formyltetrahydrofolate Oryctolagus cuniculus
1.5.1.6 10-formyltetrahydrofolate pentaglutamate form as coenzyme is very tightly bound to enzyme Oryctolagus cuniculus
1.5.1.6 folate 10-formyl-5,8-dideazafolate and 5,8-dideazafolate Oryctolagus cuniculus
1.5.1.6 NADP+
-
 Oryctolagus cuniculus
1.5.1.6 tetrahydrofolate
-
 Oryctolagus cuniculus