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Literature summary for 1.17.1.9 extracted from

  • Karagueler, N.G.; Sessions, R.B.; Clarke, A.R.
    Effects of disulphide bridges on the activity and stability of the formate dehydrogenase from Candida methylica (2007), Biotechnol. Lett., 29, 1375-1380.
    View publication on PubMed
Search for more literature for 1.17.1.9

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli [Candida] methylica

Protein Variants

Protein Variants Comment Organism
M156C/L159C no FDH activity [Candida] methylica
T169C/T226C mutant is less active and less thermostable than wild type FDH [Candida] methylica
V88C/V112C no FDH activity [Candida] methylica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.63
-
 formate wild type enzyme, at 20°C, in 20 mM triethanolamine at pH 8 [Candida] methylica
6
-
 formate oxidized mutant enzyme T169C/T226C, at 20°C, in 20 mM triethanolamine at pH 8 [Candida] methylica
10.8
-
 formate reduced mutant enzyme T169C/T226C, at 20°C, in 20 mM triethanolamine at pH 8 [Candida] methylica

Organism

Organism UniProt Comment Textmining
[Candida] methylica
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 [Candida] methylica

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
FDH
-
 [Candida] methylica

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.29
-
 formate oxidized mutant enzyme T169C/T226C, at 20°C, in 20 mM triethanolamine at pH 8 [Candida] methylica
0.5
-
 formate reduced mutant enzyme T169C/T226C, at 20°C, in 20 mM triethanolamine at pH 8 [Candida] methylica
1.2
-
 formate wild type enzyme, at 20°C, in 20 mM triethanolamine at pH 8 [Candida] methylica

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 [Candida] methylica