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show all sequences of 1.1.1.119

Alteration of coenzyme specificity in halophilic NAD(P)+ glucose dehydrogenase by site-directed mutagenesis

Pire, C.; Esclapez, J.; Diaz, S.; Perez-Pomares, F.; Ferrer, J.; Bonete, M.; J. Mol. Catal. B 59, 261-265 (2009)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed as recombinant protein in Escherichia coli strain BL21(DE3); expressed in Escherichia coli BL21 (DE3) cells; expression as inclusion bodies in Escherichia coli
Haloferax mediterranei
Engineering
Amino acid exchange
Commentary
Organism
G206D
less efficient with NADP+ than the wild type, 1.6fold increase in ratio kcat/Km for NAD+; prefers NAD+ over NADP+; the mutant is less efficient with NADP+ than the wild type enzyme, the relation kcat/KNAD+ is 1.6times higher than in the wild type, resulting in an enzyme that prefers NAD+ over NADP+
Haloferax mediterranei
G206D/R207I
active only with NAD+; no activity with NADP+, highest reaction rate with cofactor NAD+ of all mutants tested; the mutant shows no activity with NADP+, when the coenzyme NAD+ is incubated with this double mutant, it reaches the highest kcat value, between 1.5 and 2times higher than the kcat of the wild type enzyme with NADP+, and between 3 and 4times higher than the kcat of the wild type with NAD+
Haloferax mediterranei
G206D/R207I/R208N
active only with NAD+; no activity with NADP+; the mutant shows no activity with NADP+
Haloferax mediterranei
R207I
less efficient with NAD+ or NADP+ than the wild-type enzyme; less efficient with NADP+ than the wild type; the mutant is less efficient with NADP+ than the wild type enzyme, shows an increase of 48times in Km value with NADP+ when compared with the wild type accompanied by a decrease in kcat, which clearly makes the R207I mutant less efficient in catalysis with NADP+, the R207I substitution also makes the enzyme less efficient with NAD+, with a decrease of 4 times in kcat/Km, this substitution also increases the Km for glucose
Haloferax mediterranei
Inhibitors
Inhibitors
Commentary
Organism
Structure
NAD(P)+
-
Haloferax mediterranei
NAD+
-
Haloferax mediterranei
NADP+
-
Haloferax mediterranei
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.035
-
NADP+
wild type enzyme; wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.035
-
NAD(P)+
with NADP+ as coenzyme
Haloferax mediterranei
0.4
-
NAD+
wild type enzyme; wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.4
-
NAD(P)+
with NAD+ as coenzyme
Haloferax mediterranei
0.49
-
NAD+
mutant enzyme G206D; mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
1.3
-
NAD+
mutant enzyme G206D/R207I/R208N; mutant enzyme R207I; mutant G206D/R207I/R208N, pH 8.8, 40°C; mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
1.7
-
NADP+
mutant enzyme R207I; mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
2.6
-
NADP+
mutant enzyme G206D; mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
2.7
-
NAD+
mutant enzyme G206D/R207I; mutant G206D/R207I, pH 8.8, 40°C
Haloferax mediterranei
2.8
-
D-glucose
wild-type, pH 8.8, 40°C; with NADP+ as coenzyme
Haloferax mediterranei
12.9
-
beta-D-glucose
wild type enzyme, using NAD+ as cosubstrate
Haloferax mediterranei
12.9
-
D-glucose
cosubstrate NAD+, wild-type, pH 8.8, 40°C; with NAD+ as coenzyme
Haloferax mediterranei
15
-
beta-D-glucose
mutant enzyme G206D, using NAD+ as cosubstrate
Haloferax mediterranei
15
-
D-glucose
cosubstrate NAD+, mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
24
-
beta-D-glucose
mutant enzyme R207I, using NADP+ as cosubstrate
Haloferax mediterranei
24
-
D-glucose
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
31.1
-
beta-D-glucose
wild type enzyme, using NADP+ as cosubstrate
Haloferax mediterranei
32
-
beta-D-glucose
mutant enzyme R207I, using NAD+ as cosubstrate
Haloferax mediterranei
32
-
D-glucose
cosubstrate NAD+, mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
52
-
beta-D-glucose
mutant enzyme G206D, using NADP+ as cosubstrate
Haloferax mediterranei
52
-
D-glucose
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
57
-
beta-D-glucose
mutant enzyme G206D/R207I/R208N, using NAD+ as cosubstrate
Haloferax mediterranei
57
-
D-glucose
cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C
Haloferax mediterranei
80
-
beta-D-glucose
mutant enzyme G206D/R207I, using NAD+ as cosubstrate
Haloferax mediterranei
80
-
D-glucose
cosubstrate NAD+, mutant G206D/R207I, pH 8.8, 40°C
Haloferax mediterranei
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Haloferax mediterranei
-
-
-
Haloferax mediterranei
Q977U7
-
-
Purification (Commentary)
Commentary
Organism
-
Haloferax mediterranei
Renatured (Commentary)
Commentary
Organism
-
Haloferax mediterranei
Storage Stability
Storage Stability
Organism
4°C, stable for weeks
Haloferax mediterranei
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
beta-D-glucose + NAD+
the enzyme has a strong preference for NADP+ over NAD+
699602
Haloferax mediterranei
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucose + NADP+
the enzyme has a strong preference for NADP+ over NAD+
699602
Haloferax mediterranei
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NAD(P)+
-
699602
Haloferax mediterranei
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
?
D-glucose + NAD+
-
699602
Haloferax mediterranei
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
-
699602
Haloferax mediterranei
D-glucono-1,5-lactone + NADH
-
-
-
?
D-glucose + NADP+
-
699602
Haloferax mediterranei
D-glucono-1,5-lactone + NADPH
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.047
-
D-glucose
cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C
Haloferax mediterranei
0.072
-
D-glucose
cosubstrate NAD+, mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
0.2
-
D-glucose
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
0.26
-
D-glucose
cosubstrate NAD+, wild-type, pH 8.8, 40°C; mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
0.5
-
D-glucose
wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.57
-
D-glucose
cosubstrate NAD+, mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
0.9
-
D-glucose
cosubstrate NAD+, mutant G206D/R207I, pH 8.8, 40°C
Haloferax mediterranei
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
poor substrate for wild-type
Haloferax mediterranei
NADP+
; the Km value of the wild type enzyme is 11fold lower for NADP+ than for NAD+, indicating that the enzyme has a strong preference for NADP+
Haloferax mediterranei
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.09
-
NADP+
wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.09
-
NAD(P)+
with NADP+ as coenzyme
Haloferax mediterranei
0.69
-
NADP+
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
1
-
NAD+
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
1.17
-
NAD+
mutant G206D/R207I, pH 8.8, 40°C
Haloferax mediterranei
1.3
-
NADP+
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
1.7
-
NAD+
mutant G206D/R207I/R208N, pH 8.8, 40°C
Haloferax mediterranei
2
-
NAD+
wild-type, pH 8.8, 40°C
Haloferax mediterranei
2
-
NAD(P)+
with NAD+ as coenzyme
Haloferax mediterranei
2.1
-
NAD+
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed as recombinant protein in Escherichia coli strain BL21(DE3); expressed in Escherichia coli BL21 (DE3) cells
Haloferax mediterranei
expression as inclusion bodies in Escherichia coli
Haloferax mediterranei
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
poor substrate for wild-type
Haloferax mediterranei
NADP+
-
Haloferax mediterranei
NADP+
the Km value of the wild type enzyme is 11fold lower for NADP+ than for NAD+, indicating that the enzyme has a strong preference for NADP+
Haloferax mediterranei
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
G206D
less efficient with NADP+ than the wild type, 1.6fold increase in ratio kcat/Km for NAD+
Haloferax mediterranei
G206D
prefers NAD+ over NADP+; the mutant is less efficient with NADP+ than the wild type enzyme, the relation kcat/KNAD+ is 1.6times higher than in the wild type, resulting in an enzyme that prefers NAD+ over NADP+
Haloferax mediterranei
G206D/R207I
no activity with NADP+, highest reaction rate with cofactor NAD+ of all mutants tested
Haloferax mediterranei
G206D/R207I
active only with NAD+; the mutant shows no activity with NADP+, when the coenzyme NAD+ is incubated with this double mutant, it reaches the highest kcat value, between 1.5 and 2times higher than the kcat of the wild type enzyme with NADP+, and between 3 and 4times higher than the kcat of the wild type with NAD+
Haloferax mediterranei
G206D/R207I/R208N
no activity with NADP+
Haloferax mediterranei
G206D/R207I/R208N
active only with NAD+; the mutant shows no activity with NADP+
Haloferax mediterranei
R207I
less efficient with NADP+ than the wild type
Haloferax mediterranei
R207I
less efficient with NAD+ or NADP+ than the wild-type enzyme; the mutant is less efficient with NADP+ than the wild type enzyme, shows an increase of 48times in Km value with NADP+ when compared with the wild type accompanied by a decrease in kcat, which clearly makes the R207I mutant less efficient in catalysis with NADP+, the R207I substitution also makes the enzyme less efficient with NAD+, with a decrease of 4 times in kcat/Km, this substitution also increases the Km for glucose
Haloferax mediterranei
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
NAD(P)+
-
Haloferax mediterranei
NAD+
-
Haloferax mediterranei
NADP+
-
Haloferax mediterranei
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.09
-
NADP+
wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.09
-
NAD(P)+
with NADP+ as coenzyme
Haloferax mediterranei
0.69
-
NADP+
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
1
-
NAD+
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
1.17
-
NAD+
mutant G206D/R207I, pH 8.8, 40°C
Haloferax mediterranei
1.3
-
NADP+
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
1.7
-
NAD+
mutant G206D/R207I/R208N, pH 8.8, 40°C
Haloferax mediterranei
2
-
NAD+
wild-type, pH 8.8, 40°C
Haloferax mediterranei
2
-
NAD(P)+
with NAD+ as coenzyme
Haloferax mediterranei
2.1
-
NAD+
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.035
-
NADP+
wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.035
-
NADP+
wild type enzyme
Haloferax mediterranei
0.035
-
NAD(P)+
with NADP+ as coenzyme
Haloferax mediterranei
0.4
-
NAD+
wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.4
-
NAD+
wild type enzyme
Haloferax mediterranei
0.4
-
NAD(P)+
with NAD+ as coenzyme
Haloferax mediterranei
0.49
-
NAD+
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
0.49
-
NAD+
mutant enzyme G206D
Haloferax mediterranei
1.3
-
NAD+
mutant G206D/R207I/R208N, pH 8.8, 40°C; mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
1.3
-
NAD+
mutant enzyme G206D/R207I/R208N; mutant enzyme R207I
Haloferax mediterranei
1.7
-
NADP+
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
1.7
-
NADP+
mutant enzyme R207I
Haloferax mediterranei
2.6
-
NADP+
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
2.6
-
NADP+
mutant enzyme G206D
Haloferax mediterranei
2.7
-
NAD+
mutant G206D/R207I, pH 8.8, 40°C
Haloferax mediterranei
2.7
-
NAD+
mutant enzyme G206D/R207I
Haloferax mediterranei
2.8
-
D-glucose
wild-type, pH 8.8, 40°C
Haloferax mediterranei
2.8
-
D-glucose
with NADP+ as coenzyme
Haloferax mediterranei
12.9
-
beta-D-glucose
wild type enzyme, using NAD+ as cosubstrate
Haloferax mediterranei
12.9
-
D-glucose
cosubstrate NAD+, wild-type, pH 8.8, 40°C
Haloferax mediterranei
12.9
-
D-glucose
with NAD+ as coenzyme
Haloferax mediterranei
15
-
beta-D-glucose
mutant enzyme G206D, using NAD+ as cosubstrate
Haloferax mediterranei
15
-
D-glucose
cosubstrate NAD+, mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
24
-
beta-D-glucose
mutant enzyme R207I, using NADP+ as cosubstrate
Haloferax mediterranei
24
-
D-glucose
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
31.1
-
beta-D-glucose
wild type enzyme, using NADP+ as cosubstrate
Haloferax mediterranei
32
-
beta-D-glucose
mutant enzyme R207I, using NAD+ as cosubstrate
Haloferax mediterranei
32
-
D-glucose
cosubstrate NAD+, mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
52
-
beta-D-glucose
mutant enzyme G206D, using NADP+ as cosubstrate
Haloferax mediterranei
52
-
D-glucose
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
57
-
beta-D-glucose
mutant enzyme G206D/R207I/R208N, using NAD+ as cosubstrate
Haloferax mediterranei
57
-
D-glucose
cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C
Haloferax mediterranei
80
-
beta-D-glucose
mutant enzyme G206D/R207I, using NAD+ as cosubstrate
Haloferax mediterranei
80
-
D-glucose
cosubstrate NAD+, mutant G206D/R207I, pH 8.8, 40°C
Haloferax mediterranei
Purification (Commentary) (protein specific)
Commentary
Organism
-
Haloferax mediterranei
Renatured (Commentary) (protein specific)
Commentary
Organism
-
Haloferax mediterranei
Storage Stability (protein specific)
Storage Stability
Organism
4°C, stable for weeks
Haloferax mediterranei
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
beta-D-glucose + NAD+
the enzyme has a strong preference for NADP+ over NAD+
699602
Haloferax mediterranei
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucose + NADP+
the enzyme has a strong preference for NADP+ over NAD+
699602
Haloferax mediterranei
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NAD(P)+
-
699602
Haloferax mediterranei
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
?
D-glucose + NAD+
-
699602
Haloferax mediterranei
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
-
699602
Haloferax mediterranei
D-glucono-1,5-lactone + NADH
-
-
-
?
D-glucose + NADP+
-
699602
Haloferax mediterranei
D-glucono-1,5-lactone + NADPH
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.047
-
D-glucose
cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C
Haloferax mediterranei
0.072
-
D-glucose
cosubstrate NAD+, mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
0.2
-
D-glucose
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
0.26
-
D-glucose
cosubstrate NAD+, wild-type, pH 8.8, 40°C; mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
0.5
-
D-glucose
wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.57
-
D-glucose
cosubstrate NAD+, mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
0.9
-
D-glucose
cosubstrate NAD+, mutant G206D/R207I, pH 8.8, 40°C
Haloferax mediterranei
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0000008
-
D-glucose
cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C
Haloferax mediterranei
0.000002
-
D-glucose
cosubstrate NAD+, mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
0.000005
-
D-glucose
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
0.000008
-
D-glucose
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
0.000012
-
D-glucose
cosubstrate NAD+, mutant G206D/R207I, pH 8.8, 40°C
Haloferax mediterranei
0.00002
-
D-glucose
cosubstrate NAD+, wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.000035
-
NAD+
mutant G206D/R207I/R208N, pH 8.8, 40°C
Haloferax mediterranei
0.000038
-
D-glucose
cosubstrate NAD+, mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
0.000055
-
NAD+
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
0.0001
-
NADP+
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
0.00012
-
NADP+
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
0.00019
-
D-glucose
wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.00033
-
NAD+
mutant G206D/R207I, pH 8.8, 40°C
Haloferax mediterranei
0.00073
-
NAD+
wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.00112
-
NAD+
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
0.015
-
NADP+
wild-type, pH 8.8, 40°C
Haloferax mediterranei
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0000008
-
D-glucose
cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C
Haloferax mediterranei
0.000002
-
D-glucose
cosubstrate NAD+, mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
0.000005
-
D-glucose
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
0.000008
-
D-glucose
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
0.000012
-
D-glucose
cosubstrate NAD+, mutant G206D/R207I, pH 8.8, 40°C
Haloferax mediterranei
0.00002
-
D-glucose
cosubstrate NAD+, wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.000035
-
NAD+
mutant G206D/R207I/R208N, pH 8.8, 40°C
Haloferax mediterranei
0.000038
-
D-glucose
cosubstrate NAD+, mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
0.000055
-
NAD+
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
0.0001
-
NADP+
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
0.00012
-
NADP+
mutant R207I, pH 8.8, 40°C
Haloferax mediterranei
0.00019
-
D-glucose
wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.00033
-
NAD+
mutant G206D/R207I, pH 8.8, 40°C
Haloferax mediterranei
0.00073
-
NAD+
wild-type, pH 8.8, 40°C
Haloferax mediterranei
0.00112
-
NAD+
mutant G206D, pH 8.8, 40°C
Haloferax mediterranei
0.015
-
NADP+
wild-type, pH 8.8, 40°C
Haloferax mediterranei
Other publictions for EC 1.1.1.119
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
728011
Sugii
Characterization of the low-te ...
Sulfolobus tokodaii, Sulfolobus tokodaii DSM 16993
J. Biosci. Bioeng.
118
367-371
2014
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699602
Pire
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Alteration of coenzyme specifi ...
Haloferax mediterranei
J. Mol. Catal. B
59
261-265
2009
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701014
Baker
Active site dynamics in the zi ...
Haloferax mediterranei
Proc. Natl. Acad. Sci. USA
106
779-784
2009
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684637
Schewe
Improvement of P450(BM-3) whol ...
Bacillus megaterium
Appl. Microbiol. Biotechnol.
78
55-65
2008
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696604
Sovic
The utilization of bathocuproi ...
Pseudomonas fluorescens
Bioorg. Chem.
36
91-95
2008
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686754
Esclapez
Analysis of acidic surface of ...
Haloferax mediterranei
FEBS Lett.
581
837-842
2007
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728653
Britton
Analysis of protein solvent in ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
Proc. Natl. Acad. Sci. USA
103
4846-4851
2006
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667073
Esclapez
Crystallization and preliminar ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
Acta Crystallogr. Sect. F
61
743-746
2005
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656318
Satoh
Enzyme-catalyzed poly(3-hydrox ...
Cupriavidus necator
J. Biosci. Bioeng.
95
335-341
2003
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285785
Johnsen
Different glycolytic pathways ...
Halococcus saccharolyticus
Arch. Microbiol.
175
52-61
2001
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726569
Ferrer
Crystallization and preliminar ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
Acta Crystallogr. Sect. D
57
1887-1889
2001
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285784
Kataoka
Escherichia coli transformant ...
Bacillus megaterium
Biosci. Biotechnol. Biochem.
62
167-169
1998
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639098
Bonete
Glucose dehydrogenase from the ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
FEBS Lett.
383
227-229
1996
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285783
Buckmann
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A different acceptance of aden ...
Bacillus megaterium, Filobasidium uniguttulatum
Biotechnol. Appl. Biochem.
14
104-113
1991
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285782
Adachi
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Crystallization and characteri ...
Gluconobacter oxydans
Agric. Biol. Chem.
44
301-308
1980
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285781
Avigad
Aldohexose dehydrogenase from ...
Gluconobacter cerinus
Methods Enzymol.
41
142-147
1975
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285780
Avigad
Purification and properties of ...
Gluconobacter cerinus
J. Biol. Chem.
243
1936-1941
1968
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