BRENDA - Enzyme Database show

Pcal_1311, an alcohol dehydrogenase homologue from Pyrobaculum calidifontis, displays NADH-dependent high aldehyde reductase activity

Ashraf, R.; Rashid, N.; Kanai, T.; Imanaka, T.; Akhtar, M.; Extremophiles FEHLT, 0000 (2017)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
1.1.1.1
Triton X-100
10% v/v, 3fold increase in activity
Pyrobaculum calidifontis
Cloned(Commentary)
EC Number
Commentary
Organism
1.1.1.1
expression in Escherichia coli
Pyrobaculum calidifontis
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.1.1.1
additional information
presence of EDTA is not significantly inhibitory. Incubation with 100 mM EDTA at 70°C for 2 h results in loss of half of the enzyme activity. The enzyme is highly stable in the presence of up to 8 M urea or up to 6 M guanidine hydrochloride
Pyrobaculum calidifontis
1.1.1.1
Sodium dodecyl sulfate
5 mM, complete loss of activity
Pyrobaculum calidifontis
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.1.1.1
0.072
-
NADH
pH 6, 60°C
Pyrobaculum calidifontis
1.1.1.1
0.36
-
1,4-Butanediol
pH 10, 60°C
Pyrobaculum calidifontis
1.1.1.1
0.67
-
Glutaraldehyde
pH 6, 60°C
Pyrobaculum calidifontis
1.1.1.1
1.7
-
NAD+
pH 10, 60°C
Pyrobaculum calidifontis
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.1.1.1
Zn2+
Pcal_1311 is contains two zinc atoms per subunit. Twofold increase in enzyme activity of Pcal_1311 when produced in the presence of 25 microM Zn2+ as compared to the protein produced in tap water
Pyrobaculum calidifontis
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.1.1.1
76000
-
gel filtration
Pyrobaculum calidifontis
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.1.1.1
Pyrobaculum calidifontis
A3MVR8
-
-
1.1.1.1
Pyrobaculum calidifontis JCM 11548
A3MVR8
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.1.1
1,2-butanediol + NAD+
-
742472
Pyrobaculum calidifontis
? + NADH + H+
-
-
-
?
1.1.1.1
1,4-butanediol + NAD+
best substrate in oxidation reaction
742472
Pyrobaculum calidifontis
? + NADH + H+
-
-
-
?
1.1.1.1
1-butanol + NAD+
-
742472
Pyrobaculum calidifontis
butanal + NADH + H+
-
-
-
?
1.1.1.1
1-butanol + NAD+
-
742472
Pyrobaculum calidifontis JCM 11548
butanal + NADH + H+
-
-
-
?
1.1.1.1
1-hexanol + NAD+
-
742472
Pyrobaculum calidifontis
hexanal + NADH + H+
-
-
-
?
1.1.1.1
1-hexanol + NAD+
-
742472
Pyrobaculum calidifontis JCM 11548
hexanal + NADH + H+
-
-
-
?
1.1.1.1
1-octanol + NAD+
-
742472
Pyrobaculum calidifontis
octanal + NADH + H+
-
-
-
?
1.1.1.1
1-octanol + NAD+
-
742472
Pyrobaculum calidifontis JCM 11548
octanal + NADH + H+
-
-
-
?
1.1.1.1
1-pentanol + NAD+
-
742472
Pyrobaculum calidifontis
pentanal + NADH + H+
-
-
-
?
1.1.1.1
acetaldehyde + NADH + H+
5.7% of the activity with glutaraldehyde
742472
Pyrobaculum calidifontis
ethanol + NAD+
-
-
-
?
1.1.1.1
acetaldehyde + NADH + H+
5.7% of the activity with glutaraldehyde
742472
Pyrobaculum calidifontis JCM 11548
ethanol + NAD+
-
-
-
?
1.1.1.1
cinnamyl alcohol + NAD+
-
742472
Pyrobaculum calidifontis
cinnamyl aldehyde + NADH + H+
-
-
-
?
1.1.1.1
ethanol + NAD+
33% of the activity with 1,4-butanediol
742472
Pyrobaculum calidifontis
acetaldehyde + NADH + H+
-
-
-
?
1.1.1.1
glutaraldehyde + NADH + H+
best substrate in reduction reaction
742472
Pyrobaculum calidifontis
? + NAD+
-
-
-
?
1.1.1.1
hexanal + NADH + H+
69.6% of the activity with glutaraldehyde
742472
Pyrobaculum calidifontis
1-hexanol + NAD+
-
-
-
?
1.1.1.1
isobutanal + NADH + H+
20% of the activity with glutaraldehyde
742472
Pyrobaculum calidifontis
isobutanol + NAD+
-
-
-
?
1.1.1.1
mannitol + NAD+
-
742472
Pyrobaculum calidifontis
? + NADH + H+
-
-
-
?
1.1.1.1
additional information
the enzyme catalyzes NAD(H)-dependent oxidation of various alcohols and reduction of aldehydes, with a marked preference for substrates with functional group at the terminal carbon atom
742472
Pyrobaculum calidifontis
?
-
-
-
-
1.1.1.1
additional information
the enzyme catalyzes NAD(H)-dependent oxidation of various alcohols and reduction of aldehydes, with a marked preference for substrates with functional group at the terminal carbon atom
742472
Pyrobaculum calidifontis JCM 11548
?
-
-
-
-
1.1.1.1
pentanal + NADH + H+
38% of the activity with glutaraldehyde
742472
Pyrobaculum calidifontis
1-pentanol + NAD+
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.1.1.1
dimer
2 * 37555, calculated
Pyrobaculum calidifontis
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.1.1.1
80
-
-
Pyrobaculum calidifontis
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
1.1.1.1
80
-
12 h, 80% residual activity
Pyrobaculum calidifontis
1.1.1.1
90
-
3 h, 90% residual activity. No significant change in the CD spectra up to 90 °C
Pyrobaculum calidifontis
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.1.1.1
1.98
-
1,4-Butanediol
pH 10, 60°C
Pyrobaculum calidifontis
1.1.1.1
93.13
-
Glutaraldehyde
pH 6, 60°C
Pyrobaculum calidifontis
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.1.1.1
6
-
sodium phosphate buffer, highest activity for reduction of acetaldehyde
Pyrobaculum calidifontis
1.1.1.1
10
-
glycine–NaOH buffer, highest activity for oxidation of ethanol
Pyrobaculum calidifontis
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.1.1.1
additional information
no activity with NADP+
Pyrobaculum calidifontis
1.1.1.1
NAD+
-
Pyrobaculum calidifontis
1.1.1.1
NADH
-
Pyrobaculum calidifontis
pI Value
EC Number
Organism
Commentary
pI Value Maximum
pI Value
1.1.1.1
Pyrobaculum calidifontis
-
-
6.6
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
1.1.1.1
Triton X-100
10% v/v, 3fold increase in activity
Pyrobaculum calidifontis
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.1.1.1
expression in Escherichia coli
Pyrobaculum calidifontis
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.1.1.1
additional information
no activity with NADP+
Pyrobaculum calidifontis
1.1.1.1
NAD+
-
Pyrobaculum calidifontis
1.1.1.1
NADH
-
Pyrobaculum calidifontis
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.1.1.1
additional information
presence of EDTA is not significantly inhibitory. Incubation with 100 mM EDTA at 70°C for 2 h results in loss of half of the enzyme activity. The enzyme is highly stable in the presence of up to 8 M urea or up to 6 M guanidine hydrochloride
Pyrobaculum calidifontis
1.1.1.1
Sodium dodecyl sulfate
5 mM, complete loss of activity
Pyrobaculum calidifontis
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.1.1.1
0.072
-
NADH
pH 6, 60°C
Pyrobaculum calidifontis
1.1.1.1
0.36
-
1,4-Butanediol
pH 10, 60°C
Pyrobaculum calidifontis
1.1.1.1
0.67
-
Glutaraldehyde
pH 6, 60°C
Pyrobaculum calidifontis
1.1.1.1
1.7
-
NAD+
pH 10, 60°C
Pyrobaculum calidifontis
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.1.1.1
Zn2+
Pcal_1311 is contains two zinc atoms per subunit. Twofold increase in enzyme activity of Pcal_1311 when produced in the presence of 25 microM Zn2+ as compared to the protein produced in tap water
Pyrobaculum calidifontis
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.1.1.1
76000
-
gel filtration
Pyrobaculum calidifontis
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.1.1
1,2-butanediol + NAD+
-
742472
Pyrobaculum calidifontis
? + NADH + H+
-
-
-
?
1.1.1.1
1,4-butanediol + NAD+
best substrate in oxidation reaction
742472
Pyrobaculum calidifontis
? + NADH + H+
-
-
-
?
1.1.1.1
1-butanol + NAD+
-
742472
Pyrobaculum calidifontis
butanal + NADH + H+
-
-
-
?
1.1.1.1
1-butanol + NAD+
-
742472
Pyrobaculum calidifontis JCM 11548
butanal + NADH + H+
-
-
-
?
1.1.1.1
1-hexanol + NAD+
-
742472
Pyrobaculum calidifontis
hexanal + NADH + H+
-
-
-
?
1.1.1.1
1-hexanol + NAD+
-
742472
Pyrobaculum calidifontis JCM 11548
hexanal + NADH + H+
-
-
-
?
1.1.1.1
1-octanol + NAD+
-
742472
Pyrobaculum calidifontis
octanal + NADH + H+
-
-
-
?
1.1.1.1
1-octanol + NAD+
-
742472
Pyrobaculum calidifontis JCM 11548
octanal + NADH + H+
-
-
-
?
1.1.1.1
1-pentanol + NAD+
-
742472
Pyrobaculum calidifontis
pentanal + NADH + H+
-
-
-
?
1.1.1.1
acetaldehyde + NADH + H+
5.7% of the activity with glutaraldehyde
742472
Pyrobaculum calidifontis
ethanol + NAD+
-
-
-
?
1.1.1.1
acetaldehyde + NADH + H+
5.7% of the activity with glutaraldehyde
742472
Pyrobaculum calidifontis JCM 11548
ethanol + NAD+
-
-
-
?
1.1.1.1
cinnamyl alcohol + NAD+
-
742472
Pyrobaculum calidifontis
cinnamyl aldehyde + NADH + H+
-
-
-
?
1.1.1.1
ethanol + NAD+
33% of the activity with 1,4-butanediol
742472
Pyrobaculum calidifontis
acetaldehyde + NADH + H+
-
-
-
?
1.1.1.1
glutaraldehyde + NADH + H+
best substrate in reduction reaction
742472
Pyrobaculum calidifontis
? + NAD+
-
-
-
?
1.1.1.1
hexanal + NADH + H+
69.6% of the activity with glutaraldehyde
742472
Pyrobaculum calidifontis
1-hexanol + NAD+
-
-
-
?
1.1.1.1
isobutanal + NADH + H+
20% of the activity with glutaraldehyde
742472
Pyrobaculum calidifontis
isobutanol + NAD+
-
-
-
?
1.1.1.1
mannitol + NAD+
-
742472
Pyrobaculum calidifontis
? + NADH + H+
-
-
-
?
1.1.1.1
additional information
the enzyme catalyzes NAD(H)-dependent oxidation of various alcohols and reduction of aldehydes, with a marked preference for substrates with functional group at the terminal carbon atom
742472
Pyrobaculum calidifontis
?
-
-
-
-
1.1.1.1
additional information
the enzyme catalyzes NAD(H)-dependent oxidation of various alcohols and reduction of aldehydes, with a marked preference for substrates with functional group at the terminal carbon atom
742472
Pyrobaculum calidifontis JCM 11548
?
-
-
-
-
1.1.1.1
pentanal + NADH + H+
38% of the activity with glutaraldehyde
742472
Pyrobaculum calidifontis
1-pentanol + NAD+
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.1.1.1
dimer
2 * 37555, calculated
Pyrobaculum calidifontis
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.1.1.1
80
-
-
Pyrobaculum calidifontis
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
1.1.1.1
80
-
12 h, 80% residual activity
Pyrobaculum calidifontis
1.1.1.1
90
-
3 h, 90% residual activity. No significant change in the CD spectra up to 90 °C
Pyrobaculum calidifontis
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.1.1.1
1.98
-
1,4-Butanediol
pH 10, 60°C
Pyrobaculum calidifontis
1.1.1.1
93.13
-
Glutaraldehyde
pH 6, 60°C
Pyrobaculum calidifontis
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.1.1.1
6
-
sodium phosphate buffer, highest activity for reduction of acetaldehyde
Pyrobaculum calidifontis
1.1.1.1
10
-
glycine–NaOH buffer, highest activity for oxidation of ethanol
Pyrobaculum calidifontis
pI Value (protein specific)
EC Number
Organism
Commentary
pI Value Maximum
pI Value
1.1.1.1
Pyrobaculum calidifontis
-
-
6.6
KCat/KM [mM/s]
EC Number
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.1.1.1
5.5
-
1,4-Butanediol
pH 10, 60°C
Pyrobaculum calidifontis
1.1.1.1
139
-
Glutaraldehyde
pH 6, 60°C
Pyrobaculum calidifontis
KCat/KM [mM/s] (protein specific)
EC Number
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.1.1.1
5.5
-
1,4-Butanediol
pH 10, 60°C
Pyrobaculum calidifontis
1.1.1.1
139
-
Glutaraldehyde
pH 6, 60°C
Pyrobaculum calidifontis