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Literature summary for 1.5.1.6 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
Search for more literature for 1.5.1.6

Activating Compound

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

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Oryctolagus cuniculus

Source Tissue

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

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