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Literature summary extracted from

  • Krupenko, S.A.; Wagner, C.
    Overexpression of functional hydrolase domain of rat liver 10-formyltetrahydrofolate dehydrogenase in Escherichia coli (1998), Protein Expr. Purif., 14, 146-152.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.6 expression of FDH and its N-terminal and C-terminal domains in insect cells, using a baculovirus expression system, expression of FDH and of its 310 amino acid residue N-terminal domain in Escherichia coli BL21 using the pRSET vector, full-length enzyme expressed in Escherichia coli is nonsoluble, because of the large size of its monomer and uncorrect folding in prokaryotic cells 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
-
4 * 99000, SDS-PAGE Rattus norvegicus

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 recombinant 310 amino acid residue N-terminal domain 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
-
Rattus norvegicus tetrahydrofolate + CO2 + NADPH + H+
-
?
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 4 * 99000, SDS-PAGE Rattus norvegicus
1.5.1.6 homotetramer monomer with 902 amino acid residues 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