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

BRENDA support

Literature summary extracted from

  • Tsybovsky, Y.; Donato, H.; Krupenko, N.I.; Davies, C.; Krupenko, S.A.
    Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: implications for the catalytic mechanism of aldehyde dehydrogenases (2007), Biochemistry, 46, 2917-2929.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.6 expressed in Escherichia coli Rattus norvegicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.1.6 C-terminal domain of FDH and its complexes with oxidized and reduced forms of NADP+ are crystallized using the hanging drop vapour diffusion method with 1.4-1.5 M ammonium sulfate and 0.1 M Tris-HCl, pH 7.0-7.5 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 Ni-NTA column chromatography 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+
-
?

Synonyms

EC Number Synonyms Comment Organism
1.5.1.6 10-formyltetrahydrofolate dehydrogenase
-
Rattus norvegicus
1.5.1.6 FDH
-
Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.6 NADP+ dependent Rattus norvegicus