BRENDA - Enzyme Database show
show all sequences of 1.1.1.119

Analysis of acidic surface of Haloferax mediterranei glucose dehydrogenase by site-directed mutagenesis

Esclapez, J.; Pire, C.; Bautista, V.; Martinez-Espinosa, R.M.; Ferrer, J.; Bonete, M.J.; FEBS Lett. 581, 837-842 (2007)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
NaCl
triple mutant D172K/D216K/D344K shows its maximum activity in a buffer with 0.50-0.75 M NaCl while the wild type protein has its maximum activity with 1.5 M NaCl
Haloferax mediterranei
Engineering
Amino acid exchange
Commentary
Organism
D172K
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
Haloferax mediterranei
D172K/D216K/D344K
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
Haloferax mediterranei
D216K
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
Haloferax mediterranei
D344K
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
Haloferax mediterranei
Inhibitors
Inhibitors
Commentary
Organism
Structure
KCl
at 40°C, half-life in 0.5 M KCl is 86 h for wild-type, and 114 h for mutant D172K/D216K/D344K, 95 h for mutant D172K, 117 h for mutant D216K, 114 h for mutant D344K. At 25°C, half-life in 0.5 M KCl is 506 h for wild-type, and 613 h for mutant D172K/D216K/D344K, 630 h for mutant D172K, 660 h for mutant D216K, 537 h for mutant D344K
Haloferax mediterranei
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.035
-
NADP+
mutant D216K; wild-type
Haloferax mediterranei
0.036
-
NADP+
mutant D172K
Haloferax mediterranei
0.046
-
NADP+
mutant D172K/D216K/D344K
Haloferax mediterranei
0.056
-
NADP+
mutant D344K
Haloferax mediterranei
1.8
-
D-glucose
mutant D344K
Haloferax mediterranei
2.2
-
D-glucose
mutant D216K
Haloferax mediterranei
2.4
-
D-glucose
mutant D172K
Haloferax mediterranei
2.8
-
D-glucose
wild-type
Haloferax mediterranei
3.2
-
D-glucose
mutant D172K/D216K/D344K
Haloferax mediterranei
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Haloferax mediterranei
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + NADP+
-
686754
Haloferax mediterranei
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00041
-
D-glucose
mutant D216K; mutant D344K
Haloferax mediterranei
0.00045
-
D-glucose
mutant D172K; mutant D172K/D216K/D344K
Haloferax mediterranei
0.00051
-
D-glucose
wild-type
Haloferax mediterranei
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Haloferax mediterranei
NADPH
-
Haloferax mediterranei
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
NaCl
triple mutant D172K/D216K/D344K shows its maximum activity in a buffer with 0.50-0.75 M NaCl while the wild type protein has its maximum activity with 1.5 M NaCl
Haloferax mediterranei
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Haloferax mediterranei
NADPH
-
Haloferax mediterranei
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D172K
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
Haloferax mediterranei
D172K/D216K/D344K
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
Haloferax mediterranei
D216K
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
Haloferax mediterranei
D344K
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
Haloferax mediterranei
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
KCl
at 40°C, half-life in 0.5 M KCl is 86 h for wild-type, and 114 h for mutant D172K/D216K/D344K, 95 h for mutant D172K, 117 h for mutant D216K, 114 h for mutant D344K. At 25°C, half-life in 0.5 M KCl is 506 h for wild-type, and 613 h for mutant D172K/D216K/D344K, 630 h for mutant D172K, 660 h for mutant D216K, 537 h for mutant D344K
Haloferax mediterranei
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.035
-
NADP+
mutant D216K; wild-type
Haloferax mediterranei
0.036
-
NADP+
mutant D172K
Haloferax mediterranei
0.046
-
NADP+
mutant D172K/D216K/D344K
Haloferax mediterranei
0.056
-
NADP+
mutant D344K
Haloferax mediterranei
1.8
-
D-glucose
mutant D344K
Haloferax mediterranei
2.2
-
D-glucose
mutant D216K
Haloferax mediterranei
2.4
-
D-glucose
mutant D172K
Haloferax mediterranei
2.8
-
D-glucose
wild-type
Haloferax mediterranei
3.2
-
D-glucose
mutant D172K/D216K/D344K
Haloferax mediterranei
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + NADP+
-
686754
Haloferax mediterranei
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00041
-
D-glucose
mutant D216K; mutant D344K
Haloferax mediterranei
0.00045
-
D-glucose
mutant D172K; mutant D172K/D216K/D344K
Haloferax mediterranei
0.00051
-
D-glucose
wild-type
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
-
-
1
-
1
-
-
12
-
-
-
2
-
2
-
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1
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-
-
-
-
4
-
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-
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12
1
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1
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1
1
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1
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12
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2
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1
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4
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12
1
-
-
-
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-
-
-
12
12
699602
Pire
-
Alteration of coenzyme specifi ...
Haloferax mediterranei
J. Mol. Catal. B
59
261-265
2009
-
-
1
-
4
-
3
25
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-
-
2
-
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1
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1
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1
6
-
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7
-
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2
10
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2
3
-
8
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3
10
34
-
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1
1
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1
6
-
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-
7
-
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-
-
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-
-
-
16
16
701014
Baker
Active site dynamics in the zi ...
Haloferax mediterranei
Proc. Natl. Acad. Sci. USA
106
779-784
2009
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1
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1
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1
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1
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684637
Schewe
Improvement of P450(BM-3) whol ...
Bacillus megaterium
Appl. Microbiol. Biotechnol.
78
55-65
2008
-
2
1
-
1
-
-
-
-
-
-
1
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1
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1
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1
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1
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1
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1
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696604
Sovic
The utilization of bathocuproi ...
Pseudomonas fluorescens
Bioorg. Chem.
36
91-95
2008
-
1
-
-
-
-
-
-
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1
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1
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686754
Esclapez
Analysis of acidic surface of ...
Haloferax mediterranei
FEBS Lett.
581
837-842
2007
1
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4
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1
9
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1
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1
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3
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1
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9
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1
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3
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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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1
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1
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5
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1
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667073
Esclapez
Crystallization and preliminar ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
Acta Crystallogr. Sect. F
61
743-746
2005
1
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1
1
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2
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6
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1
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1
1
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1
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2
1
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2
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2
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1
1
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-
656318
Satoh
Enzyme-catalyzed poly(3-hydrox ...
Cupriavidus necator
J. Biosci. Bioeng.
95
335-341
2003
-
1
-
-
-
-
-
-
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-
-
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1
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285785
Johnsen
Different glycolytic pathways ...
Halococcus saccharolyticus
Arch. Microbiol.
175
52-61
2001
-
-
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3
-
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1
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1
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1
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3
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1
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1
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-
726569
Ferrer
Crystallization and preliminar ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
Acta Crystallogr. Sect. D
57
1887-1889
2001
-
-
1
1
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5
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1
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1
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285784
Kataoka
Escherichia coli transformant ...
Bacillus megaterium
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62
167-169
1998
-
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1
-
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1
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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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-
-
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1
3
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5
2
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9
-
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1
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1
1
4
1
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1
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2
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2
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1
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3
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5
2
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1
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1
1
4
1
-
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1
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-
-
-
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-
285783
Buckmann
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A different acceptance of aden ...
Bacillus megaterium, Filobasidium uniguttulatum
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7
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285782
Adachi
-
Crystallization and characteri ...
Gluconobacter oxydans
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44
301-308
1980
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1
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5
2
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2
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1
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1
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1
1
2
1
1
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1
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285781
Avigad
Aldohexose dehydrogenase from ...
Gluconobacter cerinus
Methods Enzymol.
41
142-147
1975
-
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2
3
5
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1
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1
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1
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4
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1
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4
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285780
Avigad
Purification and properties of ...
Gluconobacter cerinus
J. Biol. Chem.
243
1936-1941
1968
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2
4
7
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1
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1
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1
2
4
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1
1
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2
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2
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2
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7
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1
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1
2
4
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1
1
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