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

BRENDA support

Literature summary for 1.5.1.6 extracted from

  • Krupenko, S.A.; Vlasov, A.P.; Wagner, C.
    On the role of conserved histidine 106 in 10-formyltetrahydrofolate dehydrogenase catalysis (2001), J. Biol. Chem., 276, 24030-24037.
    View publication on PubMed
Search for more literature for 1.5.1.6

Cloned(Commentary)

Cloned (Comment) Organism
expression of H106K mutant of FDH in insect cells SF9, using a baculovirus expression system, and of N-terminal domain mutants in Escherichia coli BL 21 Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
H106A insoluble recombinant protein Rattus norvegicus
H106K 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
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of N-terminal domain mutants and of a H106K mutant of FDH Rattus norvegicus

Reaction

Reaction Comment Organism Reaction ID
10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH + H+ reaction mechanism Rattus norvegicus
a

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 His-106 is involved in enzyme catalysis and in folding of the N-terminal domain, enzyme requires Cys-707 for catalysis, which is located inside the C-terminal domain, mechanism includes hydrolase reaction as essential part Rattus norvegicus tetrahydrofolate + CO2 + NADPH + H+
-
 ?
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