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Literature summary extracted from

  • Wagner, C.; Briggs, W.T.; Horne, D.H.; Cook, R.J.
    10-Formyltetrahydrofolate dehydrogenase: Identification of the natural folate ligand, covalent labeling, and partial tryptic digestion (1995), Arch. Biochem. Biophys., 316, 141-147.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.6 FDH is cloned Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.6 5-formyltetrahydrofolate covalent attachment completely inhibits Rattus norvegicus
1.5.1.6 tetrahydrofolate potent, competitive product inhibitor Rattus norvegicus
1.5.1.6 tetrahydrofolate
-
 Sus scrofa
1.5.1.6 Trypsin 20 min, 70% inhibition, rapid but incomplete loss of dehydrogenase activity; tryptic digestion inactivates 10-formyltetrahydrofolate dehydrogenase but not hydrolase activity Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.5.1.6 cytosol
-
 Rattus norvegicus 5829
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.6 99000
-
 x * 99000, SDS-PAGE Rattus norvegicus

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 Sus scrofa
-
 tetrahydrofolate + CO2 + NADPH + H+
-
 ?
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O Rattus norvegicus a major folate-binding protein of liver cytosol, 10-formyltetrahydrofolate polyglutamates are tightly bound in vivo tetrahydrofolate + CO2 + NADPH + H+
-
 ?
1.5.1.6 10-formyltetrahydropteroylhexaglutamate + NADP+ + H2O Sus scrofa
-
 tetrahydropteroylhexaglutamate + CO2 + NADPH
-
 ?
1.5.1.6 10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O Rattus norvegicus
-
 tetrahydropteroylpentaglutamate + CO2 + NADPH
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.6 Rattus norvegicus
-
-
-
1.5.1.6 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.6
-
 Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.6 liver
-
 Rattus norvegicus
-
1.5.1.6 liver
-
 Sus scrofa
-

Storage Stability

EC Number Storage Stability Organism
1.5.1.6 -20°C, 20% glycerol, over 12 months, no loss of activity Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O
-
 Sus scrofa tetrahydrofolate + CO2 + NADPH + H+
-
 ?
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O
-
 Sus scrofa tetrahydrofolate + CO2 + NADPH + H+ very tight binding of product, binds its product rather than its substrate ?
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O 10-formyltetrahydrofolate is associated with enzyme when it is rapidly isolated, after storage for 24 h before separation of the binding proteins there remains none and tetrahydrofolate is the predominant form bound to enzyme because of the hydrolase activity Rattus norvegicus tetrahydrofolate + CO2 + NADPH + H+ very tight binding of product, binds its product rather than its substrate ?
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O a major folate-binding protein of liver cytosol, 10-formyltetrahydrofolate polyglutamates are tightly bound in vivo Rattus norvegicus tetrahydrofolate + CO2 + NADPH + H+
-
 ?
1.5.1.6 10-formyltetrahydropteroylhexaglutamate + NADP+ + H2O
-
 Sus scrofa tetrahydropteroylhexaglutamate + CO2 + NADPH
-
 ?
1.5.1.6 10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
-
 Rattus norvegicus tetrahydropteroylpentaglutamate + CO2 + NADPH
-
 ?
1.5.1.6 additional information
-
 Sus scrofa ?
-
 ?
1.5.1.6 additional information enzyme exhibit additional to 10-formyltetrahydrofolate dehydrogenase/hydrolase activities NADP+-dependent aldehyde dehydrogenase activity with propanal as preferred substrate Rattus norvegicus ?
-
 ?
1.5.1.6 additional information hydrolysis at 25% of dehydrogenase activity Rattus norvegicus ?
-
 ?
1.5.1.6 additional information 10-formyltetrahydrofolate dehydrogenase/hydrolase activities occur at the same time and are associated with separate active sites Rattus norvegicus ?
-
 ?
1.5.1.6 additional information irreversible covalent linkage of 5-formyltetrahydrofolate to enzyme, 2 mol bound per mol of enzyme monomer, 5-formyltetrahydrofolate is not the natural substrate and arises from 10-formyltetrahydrofolate Rattus norvegicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.1.6 ? x * 99000, SDS-PAGE Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.6 10-formyltetrahydrofolate 10-formyltetrahydrofolate Rattus norvegicus
1.5.1.6 10-formyltetrahydrofolate 10-formyltetrahydrofolate Sus scrofa
1.5.1.6 5-formyltetrahydrofolate covalent linkage of 5-formyltetrahydrofolate to enzyme, 2 mol bound per mol of enzyme monomer, it is a minor form of the folate coenzymes and arises from 10-formyltetrahydrofolate Rattus norvegicus
1.5.1.6 folate 2 mol of folate bound per mol of enzyme monomer, consistent with the presence of two active sites Rattus norvegicus
1.5.1.6 NADP+ NADP+-dependent Rattus norvegicus
1.5.1.6 NADP+ NADP+-dependent Sus scrofa
1.5.1.6 tetrahydrofolate very tight binding Rattus norvegicus
1.5.1.6 tetrahydrofolate very tight binding Sus scrofa