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Literature summary for 1.5.1.6 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
Search for more literature for 1.5.1.6

Cloned(Commentary)

Cloned (Comment) Organism
FDH is cloned Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
5-formyltetrahydrofolate covalent attachment completely inhibits Rattus norvegicus
tetrahydrofolate potent, competitive product inhibitor Rattus norvegicus
tetrahydrofolate
-
 Sus scrofa
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

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
10-formyltetrahydrofolate + NADP+ + H2O Sus scrofa
-
 tetrahydrofolate + CO2 + NADPH + H+
-
 ?
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+
-
 ?
10-formyltetrahydropteroylhexaglutamate + NADP+ + H2O Sus scrofa
-
 tetrahydropteroylhexaglutamate + CO2 + NADPH
-
 ?
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O Rattus norvegicus
-
 tetrahydropteroylpentaglutamate + CO2 + NADPH
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-
liver
-
 Sus scrofa
-

Storage Stability

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
10-formyltetrahydrofolate + NADP+ + H2O
-
 Sus scrofa tetrahydrofolate + CO2 + NADPH + H+
-
 ?
10-formyltetrahydrofolate + NADP+ + H2O
-
 Sus scrofa tetrahydrofolate + CO2 + NADPH + H+ very tight binding of product, binds its product rather than its substrate ?
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 ?
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+
-
 ?
10-formyltetrahydropteroylhexaglutamate + NADP+ + H2O
-
 Sus scrofa tetrahydropteroylhexaglutamate + CO2 + NADPH
-
 ?
10-formyltetrahydropteroylpentaglutamate + NADP+ + H2O
-
 Rattus norvegicus tetrahydropteroylpentaglutamate + CO2 + NADPH
-
 ?
additional information
-
 Sus scrofa ?
-
 ?
additional information enzyme exhibit additional to 10-formyltetrahydrofolate dehydrogenase/hydrolase activities NADP+-dependent aldehyde dehydrogenase activity with propanal as preferred substrate Rattus norvegicus ?
-
 ?
additional information hydrolysis at 25% of dehydrogenase activity Rattus norvegicus ?
-
 ?
additional information 10-formyltetrahydrofolate dehydrogenase/hydrolase activities occur at the same time and are associated with separate active sites Rattus norvegicus ?
-
 ?
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

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

Cofactor

Cofactor Comment Organism Structure
10-formyltetrahydrofolate 10-formyltetrahydrofolate Rattus norvegicus
10-formyltetrahydrofolate 10-formyltetrahydrofolate Sus scrofa
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
folate 2 mol of folate bound per mol of enzyme monomer, consistent with the presence of two active sites Rattus norvegicus
NADP+ NADP+-dependent Rattus norvegicus
NADP+ NADP+-dependent Sus scrofa
tetrahydrofolate very tight binding Rattus norvegicus
tetrahydrofolate very tight binding Sus scrofa