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Literature summary extracted from

  • Krupenko, S.A.; Wagner, C.
    Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic centers of 10-formyltetrahydrofolate dehydrogenase (1999), J. Biol. Chem., 274, 35777-35784.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.6 expression of D124A mutant of FDH and N-terminal domain mutants in Sf9 insect cells, using a baculovirus expression system Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.5.1.6 D142A mutant with a complete loss of 10-formyltetrahydrofolate dehydrogenase and hydrolase activity, aldehyde dehydrogenase activity is similar to wild-type FDH Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.5.1.6 cytosol
-
 Rattus norvegicus 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 Rattus norvegicus recycling of excess 10-formyltetrahydrofolate that is not needed for purine biosynthesis and restoration of the tetrahydrofolate pool, important for formate metabolism by clearing it as CO2 and thus protecting cells from formate intoxication tetrahydrofolate + CO2 + NADPH + H+
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.6 purification of N-terminal domain mutants and of a D124A mutant of FDH Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.6 liver
-
 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 Asp-142 is an essential residue in enzyme mechanism, it influences folate binding, model of substrate binding pocket Rattus norvegicus tetrahydrofolate + CO2 + NADPH + H+
-
 ?
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O structure of enzyme domains and of catalytic centers Rattus norvegicus tetrahydrofolate + CO2 + NADPH + H+
-
 ?
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O recycling of excess 10-formyltetrahydrofolate that is not needed for purine biosynthesis and restoration of the tetrahydrofolate pool, important for formate metabolism by clearing it as CO2 and thus protecting cells from formate intoxication Rattus norvegicus tetrahydrofolate + CO2 + NADPH + H+
-
 ?
1.5.1.6 additional information 2fold higher 10-formyltetrahydrofolate dehydrogenase than hydrolase activity, hydrolase and dehydrogenase catalytic centers are overlapping Rattus norvegicus ?
-
 ?
1.5.1.6 additional information 310 amino acid residue N-terminal domain has 10-formyltetrahydrofolate hydrolase activity and substrate binding site, C-terminal domain has aldehyde dehydrogenase activity and is used as catalytic center in dehydrogenase reaction, full-length enzyme is required for 10-formyltetrahydrofolate dehydrogenase activity, the two domains work in concert Rattus norvegicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.1.6 homotetramer monomer with 902 amino acid residues Rattus norvegicus

Temperature Optimum [°C]

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.6 10-formyltetrahydrofolate 10-formyltetrahydrofolate Rattus norvegicus
1.5.1.6 NADP+ NADP+-dependent Rattus norvegicus
1.5.1.6 tetrahydrofolate
-
 Rattus norvegicus