Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.5.1.6 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
Search for more literature for 1.5.1.6

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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+
-
 ?
10-formyltetrahydrofolate + NADP+ + H2O structure of enzyme domains and of catalytic centers Rattus norvegicus tetrahydrofolate + CO2 + NADPH + H+
-
 ?
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+
-
 ?
additional information 2fold higher 10-formyltetrahydrofolate dehydrogenase than hydrolase activity, hydrolase and dehydrogenase catalytic centers are overlapping Rattus norvegicus ?
-
 ?
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

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

Temperature Optimum [°C]

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

Cofactor

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