BRENDA - Enzyme Database show
show all sequences of 1.1.1.119

Characterization of the low-temperature activity of Sulfolobus tokodaii glucose-1-dehydrogenase mutants

Sugii, T.; Akanuma, S.; Yagi S.; Yagyu, K.; Shimoda, Y.; Yamagishi, A.; J. Biosci. Bioeng. 118, 367-371 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Sulfolobus tokodaii
Engineering
Amino acid exchange
Commentary
Organism
V254I
mutant has improved kcat and kcat/Km values at both 25C and 80C. The thermal stability of the mutant enzyme was comparable to that of the wild-type enzyme. Calculation of the energetic contribution of the V254I mutation for the dehydrogenase reaction reveals that the mutation destabilizes the enzyme-NADPD-glucose ternary complex and reduces the transition-state energy, thus enhancing catalysis
Sulfolobus tokodaii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00588
-
NADP+
pH 9.0, 25C, wild-type enzyme
Sulfolobus tokodaii
0.00876
-
NADP+
pH 9.0, 25C, mutant enzyme V254I
Sulfolobus tokodaii
0.00927
-
NADP+
pH 9.0, 25C, mutant enzyme I189V
Sulfolobus tokodaii
0.0286
-
D-glucose
pH 9.0, 25C, wild-type enzyme
Sulfolobus tokodaii
0.0293
-
D-glucose
pH 9.0, 25C, mutant enzyme I189V
Sulfolobus tokodaii
0.0391
-
D-glucose
pH 9.0, 25C, mutant enzyme V254I
Sulfolobus tokodaii
0.109
-
NADP+
pH 9.0, 80C, mutant enzyme I189V
Sulfolobus tokodaii
0.117
-
NADP+
pH 9.0, 80C, wild-type enzyme
Sulfolobus tokodaii
0.132
-
NADP+
pH 9.0, 80C, mutant enzyme V254I
Sulfolobus tokodaii
0.287
-
D-glucose
pH 9.0, 80C, wild-type enzyme
Sulfolobus tokodaii
0.314
-
D-glucose
pH 9.0, 80C, mutant enzyme I189V
Sulfolobus tokodaii
0.457
-
D-glucose
pH 9.0, 80C, mutant enzyme V254I
Sulfolobus tokodaii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + NADP+
Sulfolobus tokodaii
-
D-glucono-1,5-lactone + NADPH + H+
-
-
?
D-glucose + NADP+
Sulfolobus tokodaii DSM 16993
-
D-glucono-1,5-lactone + NADPH + H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sulfolobus tokodaii
Q96ZY7
-
-
Sulfolobus tokodaii DSM 16993
Q96ZY7
-
-
Purification (Commentary)
Commentary
Organism
-
Sulfolobus tokodaii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + NADP+
-
728011
Sulfolobus tokodaii
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
the enzyme prefers NADP+ over NAD+ as the cofactor. It shows a larger Km value for NAD+ (4.5 mM) than for NADP+ (0.12 mM) at 80C. At 25C the Km values are 0.069 mM for NAD+ and 0.0059 mM for NADP+
728011
Sulfolobus tokodaii
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
-
728011
Sulfolobus tokodaii DSM 16993
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
the enzyme prefers NADP+ over NAD+ as the cofactor. It shows a larger Km value for NAD+ (4.5 mM) than for NADP+ (0.12 mM) at 80C. At 25C the Km values are 0.069 mM for NAD+ and 0.0059 mM for NADP+
728011
Sulfolobus tokodaii DSM 16993
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
0.085
-
D-glucose
pH 9.0, 25C, mutant enzyme I189V
Sulfolobus tokodaii
0.085
-
NADP+
pH 9.0, 25C, mutant enzyme I189V
Sulfolobus tokodaii
0.11
-
D-glucose
pH 9.0, 25C, wild-type enzyme
Sulfolobus tokodaii
0.11
-
NADP+
pH 9.0, 25C, wild-type enzyme
Sulfolobus tokodaii
0.205
-
D-glucose
pH 9.0, 25C, mutant enzyme V254I
Sulfolobus tokodaii
0.205
-
NADP+
pH 9.0, 25C, mutant enzyme V254I
Sulfolobus tokodaii
9.7
-
D-glucose
pH 9.0, 80C, mutant enzyme I189V
Sulfolobus tokodaii
9.7
-
NADP+
pH 9.0, 80C, mutant enzyme I189V
Sulfolobus tokodaii
10.1
-
D-glucose
pH 9.0, 80C, wild-type enzyme
Sulfolobus tokodaii
10.1
-
NADP+
pH 9.0, 80C, wild-type enzyme
Sulfolobus tokodaii
16.7
-
D-glucose
pH 9.0, 80C, mutant enzyme V254I
Sulfolobus tokodaii
16.7
-
NADP+
pH 9.0, 80C, mutant enzyme V254I
Sulfolobus tokodaii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
assay at
Sulfolobus tokodaii
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
the enzyme prefers NADP+ over NAD+ as the cofactor. It shows a larger Km value for NAD+ (4.5 mM) than for NADP+ (0.12 mM) at 80C. At 25C the Km values are 0.069 mM for NAD+ and 0.0059 mM for NADP+
Sulfolobus tokodaii
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Sulfolobus tokodaii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
the enzyme prefers NADP+ over NAD+ as the cofactor. It shows a larger Km value for NAD+ (4.5 mM) than for NADP+ (0.12 mM) at 80C. At 25C the Km values are 0.069 mM for NAD+ and 0.0059 mM for NADP+
Sulfolobus tokodaii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
V254I
mutant has improved kcat and kcat/Km values at both 25C and 80C. The thermal stability of the mutant enzyme was comparable to that of the wild-type enzyme. Calculation of the energetic contribution of the V254I mutation for the dehydrogenase reaction reveals that the mutation destabilizes the enzyme-NADPD-glucose ternary complex and reduces the transition-state energy, thus enhancing catalysis
Sulfolobus tokodaii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00588
-
NADP+
pH 9.0, 25C, wild-type enzyme
Sulfolobus tokodaii
0.00876
-
NADP+
pH 9.0, 25C, mutant enzyme V254I
Sulfolobus tokodaii
0.00927
-
NADP+
pH 9.0, 25C, mutant enzyme I189V
Sulfolobus tokodaii
0.0286
-
D-glucose
pH 9.0, 25C, wild-type enzyme
Sulfolobus tokodaii
0.0293
-
D-glucose
pH 9.0, 25C, mutant enzyme I189V
Sulfolobus tokodaii
0.0391
-
D-glucose
pH 9.0, 25C, mutant enzyme V254I
Sulfolobus tokodaii
0.109
-
NADP+
pH 9.0, 80C, mutant enzyme I189V
Sulfolobus tokodaii
0.117
-
NADP+
pH 9.0, 80C, wild-type enzyme
Sulfolobus tokodaii
0.132
-
NADP+
pH 9.0, 80C, mutant enzyme V254I
Sulfolobus tokodaii
0.287
-
D-glucose
pH 9.0, 80C, wild-type enzyme
Sulfolobus tokodaii
0.314
-
D-glucose
pH 9.0, 80C, mutant enzyme I189V
Sulfolobus tokodaii
0.457
-
D-glucose
pH 9.0, 80C, mutant enzyme V254I
Sulfolobus tokodaii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + NADP+
Sulfolobus tokodaii
-
D-glucono-1,5-lactone + NADPH + H+
-
-
?
D-glucose + NADP+
Sulfolobus tokodaii DSM 16993
-
D-glucono-1,5-lactone + NADPH + H+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Sulfolobus tokodaii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + NADP+
-
728011
Sulfolobus tokodaii
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
the enzyme prefers NADP+ over NAD+ as the cofactor. It shows a larger Km value for NAD+ (4.5 mM) than for NADP+ (0.12 mM) at 80C. At 25C the Km values are 0.069 mM for NAD+ and 0.0059 mM for NADP+
728011
Sulfolobus tokodaii
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
-
728011
Sulfolobus tokodaii DSM 16993
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
the enzyme prefers NADP+ over NAD+ as the cofactor. It shows a larger Km value for NAD+ (4.5 mM) than for NADP+ (0.12 mM) at 80C. At 25C the Km values are 0.069 mM for NAD+ and 0.0059 mM for NADP+
728011
Sulfolobus tokodaii DSM 16993
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
0.085
-
D-glucose
pH 9.0, 25C, mutant enzyme I189V
Sulfolobus tokodaii
0.085
-
NADP+
pH 9.0, 25C, mutant enzyme I189V
Sulfolobus tokodaii
0.11
-
D-glucose
pH 9.0, 25C, wild-type enzyme
Sulfolobus tokodaii
0.11
-
NADP+
pH 9.0, 25C, wild-type enzyme
Sulfolobus tokodaii
0.205
-
D-glucose
pH 9.0, 25C, mutant enzyme V254I
Sulfolobus tokodaii
0.205
-
NADP+
pH 9.0, 25C, mutant enzyme V254I
Sulfolobus tokodaii
9.7
-
D-glucose
pH 9.0, 80C, mutant enzyme I189V
Sulfolobus tokodaii
9.7
-
NADP+
pH 9.0, 80C, mutant enzyme I189V
Sulfolobus tokodaii
10.1
-
D-glucose
pH 9.0, 80C, wild-type enzyme
Sulfolobus tokodaii
10.1
-
NADP+
pH 9.0, 80C, wild-type enzyme
Sulfolobus tokodaii
16.7
-
D-glucose
pH 9.0, 80C, mutant enzyme V254I
Sulfolobus tokodaii
16.7
-
NADP+
pH 9.0, 80C, mutant enzyme V254I
Sulfolobus tokodaii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
assay at
Sulfolobus tokodaii
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.092
-
NADP+
pH 9.0, 25C, mutant enzyme I189V
Sulfolobus tokodaii
0.126
-
NADP+
pH 9.0, 80C, mutant enzyme V254I
Sulfolobus tokodaii
0.186
-
NADP+
pH 9.0, 25C, wild-type enzyme
Sulfolobus tokodaii
0.234
-
NADP+
pH 9.0, 25C, mutant enzyme V254I
Sulfolobus tokodaii
0.31
-
D-glucose
pH 9.0, 80C, mutant enzyme I189V
Sulfolobus tokodaii
0.351
-
D-glucose
pH 9.0, 80C, wild-type enzyme
Sulfolobus tokodaii
0.365
-
D-glucose
pH 9.0, 80C, mutant enzyme V254I
Sulfolobus tokodaii
0.863
-
NADP+
pH 9.0, 80C, wild-type enzyme
Sulfolobus tokodaii
0.893
-
NADP+
pH 9.0, 80C, mutant enzyme I189V
Sulfolobus tokodaii
2.91
-
D-glucose
pH 9.0, 25C, mutant enzyme I189V
Sulfolobus tokodaii
3.82
-
D-glucose
pH 9.0, 25C, wild-type enzyme
Sulfolobus tokodaii
5.25
-
D-glucose
pH 9.0, 25C, mutant enzyme V254I
Sulfolobus tokodaii
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.092
-
NADP+
pH 9.0, 25C, mutant enzyme I189V
Sulfolobus tokodaii
0.126
-
NADP+
pH 9.0, 80C, mutant enzyme V254I
Sulfolobus tokodaii
0.186
-
NADP+
pH 9.0, 25C, wild-type enzyme
Sulfolobus tokodaii
0.234
-
NADP+
pH 9.0, 25C, mutant enzyme V254I
Sulfolobus tokodaii
0.31
-
D-glucose
pH 9.0, 80C, mutant enzyme I189V
Sulfolobus tokodaii
0.351
-
D-glucose
pH 9.0, 80C, wild-type enzyme
Sulfolobus tokodaii
0.365
-
D-glucose
pH 9.0, 80C, mutant enzyme V254I
Sulfolobus tokodaii
0.863
-
NADP+
pH 9.0, 80C, wild-type enzyme
Sulfolobus tokodaii
0.893
-
NADP+
pH 9.0, 80C, mutant enzyme I189V
Sulfolobus tokodaii
2.91
-
D-glucose
pH 9.0, 25C, mutant enzyme I189V
Sulfolobus tokodaii
3.82
-
D-glucose
pH 9.0, 25C, wild-type enzyme
Sulfolobus tokodaii
5.25
-
D-glucose
pH 9.0, 25C, mutant enzyme V254I
Sulfolobus tokodaii
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
-
-
1
-
-
-
-
-
4
-
-
-
-
12
1
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
12
-
-
-
2
-
-
-
1
-
-
-
-
4
-
-
-
-
12
1
-
-
-
-
-
-
-
12
12
699602
Pire
-
Alteration of coenzyme specifi ...
Haloferax mediterranei
J. Mol. Catal. B
59
261-265
2009
-
-
1
-
4
-
3
25
-
-
-
-
-
2
-
-
1
-
1
-
-
1
6
-
-
-
-
7
-
-
-
2
10
-
-
-
-
2
3
-
8
-
-
3
10
34
-
-
-
-
-
-
-
1
1
-
-
1
6
-
-
-
-
7
-
-
-
-
-
-
-
-
16
16
701014
Baker
Active site dynamics in the zi ...
Haloferax mediterranei
Proc. Natl. Acad. Sci. USA
106
779-784
2009
-
-
-
1
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684637
Schewe
Improvement of P450(BM-3) whol ...
Bacillus megaterium
Appl. Microbiol. Biotechnol.
78
55-65
2008
-
2
1
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
696604
Sovic
The utilization of bathocuproi ...
Pseudomonas fluorescens
Bioorg. Chem.
36
91-95
2008
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
686754
Esclapez
Analysis of acidic surface of ...
Haloferax mediterranei
FEBS Lett.
581
837-842
2007
1
-
-
-
4
-
1
9
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
2
-
-
-
1
-
-
2
-
4
-
-
1
-
9
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
728653
Britton
Analysis of protein solvent in ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
Proc. Natl. Acad. Sci. USA
103
4846-4851
2006
-
-
-
1
-
-
-
-
-
1
-
-
-
5
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
667073
Esclapez
Crystallization and preliminar ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
Acta Crystallogr. Sect. F
61
743-746
2005
1
-
-
1
1
-
-
-
-
-
2
-
-
6
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
1
-
-
1
2
1
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656318
Satoh
Enzyme-catalyzed poly(3-hydrox ...
Cupriavidus necator
J. Biosci. Bioeng.
95
335-341
2003
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285785
Johnsen
Different glycolytic pathways ...
Halococcus saccharolyticus
Arch. Microbiol.
175
52-61
2001
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
726569
Ferrer
Crystallization and preliminar ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
Acta Crystallogr. Sect. D
57
1887-1889
2001
-
-
1
1
-
-
-
-
-
-
-
-
-
5
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285784
Kataoka
Escherichia coli transformant ...
Bacillus megaterium
Biosci. Biotechnol. Biochem.
62
167-169
1998
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
639098
Bonete
Glucose dehydrogenase from the ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
FEBS Lett.
383
227-229
1996
-
-
-
-
-
-
1
3
-
5
2
-
-
9
-
-
1
-
-
-
1
1
4
1
-
-
1
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
1
-
3
-
5
2
-
-
-
-
1
-
-
1
1
4
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
285783
Buckmann
-
A different acceptance of aden ...
Bacillus megaterium, Filobasidium uniguttulatum
Biotechnol. Appl. Biochem.
14
104-113
1991
-
-
-
-
-
-
-
5
-
-
-
-
-
2
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
5
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285782
Adachi
-
Crystallization and characteri ...
Gluconobacter oxydans
Agric. Biol. Chem.
44
301-308
1980
-
-
-
1
-
-
5
2
-
-
2
-
-
1
-
-
1
-
-
-
1
1
2
1
1
-
-
-
1
-
-
2
-
-
-
-
-
-
2
1
-
-
-
5
-
2
-
-
2
-
-
-
-
1
-
-
1
1
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
285781
Avigad
Aldohexose dehydrogenase from ...
Gluconobacter cerinus
Methods Enzymol.
41
142-147
1975
-
-
-
-
-
2
3
5
-
-
-
-
-
1
-
-
1
-
-
-
1
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
2
-
3
-
5
-
-
-
-
-
-
-
1
-
-
1
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285780
Avigad
Purification and properties of ...
Gluconobacter cerinus
J. Biol. Chem.
243
1936-1941
1968
-
-
-
-
-
2
4
7
-
-
-
-
-
1
-
-
1
-
-
-
1
2
4
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
2
-
-
2
-
4
-
7
-
-
-
-
-
-
-
1
-
-
1
2
4
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-