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

BRENDA support

Literature summary for 1.17.1.9 extracted from

  • Ordu, E.; Sessions, R.; Clarke, A.; Karagüler, N.
    Effect of surface electrostatic interactions on the stability and folding of formate dehydrogenase from Candida methylica (2013), J. Mol. Catal. B, 95, 23-28.
No PubMed abstract available
Search for more literature for 1.17.1.9

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia JM105 cells [Candida] methylica

Protein Variants

Protein Variants Comment Organism
H13E the mutant shows decreased catalytic efficiency compared to the wild type enzyme [Candida] methylica
N147R the mutant shows decreased catalytic efficiency compared to the wild type enzyme [Candida] methylica
N187E the mutant shows decreased catalytic efficiency compared to the wild type enzyme [Candida] methylica
N187E/N147R the mutant shows decreased catalytic efficiency compared to the wild type enzyme [Candida] methylica
N187E/Q105R the mutant shows decreased catalytic efficiency compared to the wild type enzyme [Candida] methylica
N300E inactive [Candida] methylica
N300E/N147R inactive [Candida] methylica
Q105R the mutant shows wild type catalytic efficiency [Candida] methylica
Y160E the mutant shows increased catalytic efficiency compared to the wild type enzyme [Candida] methylica
Y160R the mutant shows decreased catalytic efficiency compared to the wild type enzyme [Candida] methylica
Y302E inactive [Candida] methylica
Y302R the mutant shows decreased catalytic efficiency compared to the wild type enzyme [Candida] methylica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3
-
 formate mutant enzyme Y160E, at pH 8.0 and 25°C [Candida] methylica
2.7
-
 formate mutant enzyme Y160R, at pH 8.0 and 25°C [Candida] methylica
3.9
-
 formate mutant enzyme N187E, at pH 8.0 and 25°C [Candida] methylica
4.4
-
 formate mutant enzyme N147R, at pH 8.0 and 25°C [Candida] methylica
4.4
-
 formate mutant enzyme Y302R, at pH 8.0 and 25°C [Candida] methylica
4.75
-
 formate wild type enzyme, at pH 8.0 and 25°C [Candida] methylica
5.1
-
 formate mutant enzyme Q105R, at pH 8.0 and 25°C [Candida] methylica
5.3
-
 formate mutant enzyme H13E, at pH 8.0 and 25°C [Candida] methylica
5.5
-
 formate mutant enzyme N187E/Q105R, at pH 8.0 and 25°C [Candida] methylica
5.9
-
 formate mutant enzyme N187E/N147R, at pH 8.0 and 25°C [Candida] methylica

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
 x * 42000, SDS-PAGE [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 Q00498
-
-

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+
-
 ?

Subunits

Subunits Comment Organism
? x * 42000, SDS-PAGE [Candida] methylica

Synonyms

Synonyms Comment Organism
FDH
-
 [Candida] methylica
NAD+-dependent formate dehydrogenase
-
 [Candida] methylica

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50 60 the wild type enzyme retains full activity after 20 min incubation at 50°C and shows 85.5 and 6.6% activity after 20 min incubation at 55 and 60°C, respectively [Candida] methylica

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.25
-
 formate mutant enzyme Y302R, at pH 8.0 and 25°C [Candida] methylica
0.3
-
 formate mutant enzyme Y160R, at pH 8.0 and 25°C [Candida] methylica
0.5
-
 formate mutant enzyme N187E/N147R, at pH 8.0 and 25°C [Candida] methylica
0.55
-
 formate mutant enzyme H13E, at pH 8.0 and 25°C [Candida] methylica
0.6
-
 formate mutant enzyme N187E/Q105R, at pH 8.0 and 25°C [Candida] methylica
0.7
-
 formate mutant enzyme N187E, at pH 8.0 and 25°C [Candida] methylica
0.8
-
 formate mutant enzyme Y160E, at pH 8.0 and 25°C [Candida] methylica
0.85
-
 formate mutant enzyme N147R, at pH 8.0 and 25°C [Candida] methylica
1.13
-
 formate wild type enzyme, at pH 8.0 and 25°C [Candida] methylica
1.2
-
 formate mutant enzyme Q105R, at pH 8.0 and 25°C [Candida] methylica

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 [Candida] methylica

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.06
-
 formate mutant enzyme Y302R, at pH 8.0 and 25°C [Candida] methylica
0.08
-
 formate mutant enzyme N187E/N147R, at pH 8.0 and 25°C [Candida] methylica
0.1
-
 formate mutant enzyme H13E, at pH 8.0 and 25°C [Candida] methylica
0.11
-
 formate mutant enzyme N187E/Q105R, at pH 8.0 and 25°C [Candida] methylica
0.11
-
 formate mutant enzyme Y160R, at pH 8.0 and 25°C [Candida] methylica
0.18
-
 formate mutant enzyme N187E, at pH 8.0 and 25°C [Candida] methylica
0.2
-
 formate mutant enzyme N147R, at pH 8.0 and 25°C [Candida] methylica
0.24
-
 formate wild type enzyme, at pH 8.0 and 25°C [Candida] methylica
0.24
-
 formate mutant enzyme Q105R, at pH 8.0 and 25°C [Candida] methylica
0.35
-
 formate mutant enzyme Y160E, at pH 8.0 and 25°C [Candida] methylica