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BRENDA support

Literature summary for 1.17.1.9 extracted from

  • Netto, C.; Nakamura, M.; Andrade, L.; Toma, H.
    Improving the catalytic activity of formate dehydrogenase from Candida boidinii by using magnetic nanoparticles (2012), J. Mol. Catal. B, 84, 136-143.
No PubMed abstract available
Search for more literature for 1.17.1.9

General Stability

General Stability Organism
formate dehydrogenase immobilized on magnetic glyoxylagarose support suffers a decrease in formate conversion with the increase in immobilization time. MagNP-APTS/FDH (enzyme on a magnetic support containing a silica gel coated magnetite core which is further silanized with a minopropyltriethoxysilane minopropyltriethoxysilane) shows increased stability when incubated for up to 1 h at 60°C and pH 7.5, while MagNP-APTS/glyoxyl-agarose/FDH (enzyme on a magnetic support consisting of magnetite-aminopropyltriethoxysilane coatedwith glyoxyl-agarose) is completely inactive after 20 min of incubation [Candida] boidinii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
formate + NAD+ [Candida] boidinii
-
 CO2 + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
[Candida] boidinii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formate + NAD+
-
 [Candida] boidinii CO2 + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
FDH
-
 [Candida] boidinii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 free enzyme [Candida] boidinii

pH Range

pH Minimum pH Maximum Comment Organism
5.5 8.5
-
 [Candida] boidinii

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 [Candida] boidinii