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Literature summary for 1.17.1.9 extracted from

  • Gul-Karaguler, N.; Sessions, R.B.; Clarke, A.R.; Holbrook, J.J.
    A single mutation in the NAD-specific formate dehydrogenase from Candida methylica allows the enzyme to use NADP (2001), Biotechnol. Lett., 23, 283-287.
No PubMed abstract available
Search for more literature for 1.17.1.9

Protein Variants

Protein Variants Comment Organism
D195S mutant enzyme also can use NADP+ as coenzyme [Candida] methylica
D195S mutant enzyme shows similar catalytic constant to wild-type in the reaction with NAD+. In contrast with wild-type, the reaction of NADP+ catalyzed by the mutant is clearly discernible [Candida] methylica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.7
-
 NAD+ mutant enzyme D195S [Candida] methylica
4.7
-
 NAD+ pH 8.0, 20°C, mutant enzyme D195S [Candida] methylica
5.5
-
 NAD+ wild-type enzyme [Candida] methylica
5.5
-
 NAD+ pH 8.0, 20°C, wild-type enzyme [Candida] methylica

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
[Candida] methylica
-
-
-

Purification (Commentary)

Purification (Comment) Organism
mutant enzyme D195S [Candida] methylica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formate + NAD+
-
 [Candida] methylica CO2 + NADH + H+
-
 ?
formate + NADP+ no reaction is catalyzed with wild-type enzyme, activity is detected with mutant enzyme D195S. The ratio of the catalytic efficiencies for NAD+ versus NADP+ for the mutant protein is 40:1 in favor of NAD+ [Candida] methylica CO2 + NADPH
-
 ?

Synonyms

Synonyms Comment Organism
NAD-specific formate dehydrogenase
-
 [Candida] methylica

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4
-
 NAD+ wild-type enzyme [Candida] methylica
1.4
-
 NAD+ pH 8.0, 20°C, wild-type enzyme [Candida] methylica
1.6
-
 NAD+ mutant enzyme S195S [Candida] methylica
1.6
-
 NAD+ pH 8.0, 20°C, mutant enzyme D195S [Candida] methylica

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 [Candida] methylica
NADP+ no reaction is catalyzed with wild-type enzyme, activity is detected with mutant enzyme D195S. The ratio of the catalytic efficiencies for NAD+ versus NADP+ for the mutant protein is 40:1 in favor of NAD+ [Candida] methylica