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Literature summary for 1.17.1.9 extracted from

  • Karagüler, N.G.; Sessions, R.B.; Moreton, K.M.; Clarke, A.R.; Holbrook, J.J.
    Estimating the energetic contribution of hydrogen bonding to the stability of Candida methylica formate dehydrogenase by using double mutant cycle (2004), Biotechnol. Lett., 26, 1137-1140.
    View publication on PubMed
Search for more literature for 1.17.1.9

Protein Variants

Protein Variants Comment Organism
T169V Km-value for formate is 55% of the wild-type value, turnover-number is 25% of the wild-type value [Candida] methylica
T169V/T226V Km-value for formate is increased 1.7fold compared to the wild-type value, turnover number is 25% of the wild-type value [Candida] methylica
T226V Km-value for formate is 104% of the wild-type value, turnover-number is 91% of the wild-type value [Candida] methylica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1
-
 formate 20°C, pH 8, mutant enzyme T69V [Candida] methylica
5.6
-
 formate 20°C, pH 8, wild-type enzyme [Candida] methylica
5.8
-
 formate 20°C, pH 8, mutant enzyme T226V [Candida] methylica
9.3
-
 formate 20°C, pH 8, mutant enzyme T69V/T226V [Candida] methylica

Organism

Organism UniProt Comment Textmining
[Candida] methylica
-
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.3
-
 formate 20°C, pH 8, mutant enzyme T69V [Candida] methylica
0.3
-
 formate 20°C, pH 8, mutant enzyme T69V/T226V [Candida] methylica
1.1
-
 formate 20°C, pH 8, mutant enzyme T226V [Candida] methylica
1.2
-
 formate 20°C, pH 8, wild-type enzyme [Candida] methylica

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 [Candida] methylica