BRENDA - Enzyme Database show
show all sequences of 1.1.1.67

Structure-guided engineering of the coenzyme specificity of Pseudomonas fluorescens mannitol 2-dehydrogenase to enable efficient utilization of NAD(H) and NADP(H)

Bubner, P.; Klimacek, M.; Nidetzky, B.; FEBS Lett. 582, 233-237 (2008)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
no activation of M2DH by bovine serum albumin
Pseudomonas fluorescens
Application
Application
Commentary
Organism
industry
redox balancing between the intracellular NADP(H) and NAD(H) based on NAD(P)(H)-dependent interconversion of mannitol and fructose by M2DH may be a useful strategy of metabolic engineering
Pseudomonas fluorescens
Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli; expression of wild-type and mutant enzymes in Escherichia coli strain JM109
Pseudomonas fluorescens
Engineering
Amino acid exchange
Commentary
Organism
D69A
site-directed mutagenesis, the mutant shows an altered cofactor specificity compared to the wild-type enzyme, which is switched to NADP(H), EC 1.1.1.138, NADP(H) is equally utilized as NAD(H); utilizes NAD(H) and NADP(H) with similar catalytic efficiencies. Uses NADP(H) almost as well as wild-type enzyme uses NAD(H)
Pseudomonas fluorescens
E68K
site-directed mutagenesis, the mutant shows an altered cofactor specificity compared to the wild-type enzyme, which is switched to NADP(H), EC 1.1.1.138, NADP(H) is preferred by 10fold over NAD(H)
Pseudomonas fluorescens
E68K/D69A
shows about a 10fold preference for NADP(H) over NAD(H), accompanied by a small decrease in catalytic efficiency for NAD(H)-dependent reactions as compared to wild-type enzyme
Pseudomonas fluorescens
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
no inhibition of M2DH by bovine serum albumin
Pseudomonas fluorescens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetic analysis, recombinant wild-type and mutant enzymes, overview
Pseudomonas fluorescens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-mannitol + NAD+
Pseudomonas fluorescens
wild-type enzyme
D-fructose + NADH + H+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas fluorescens
O08355
-
-
Purification (Commentary)
Commentary
Organism
mutants purified to apparent homogeneity
Pseudomonas fluorescens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-mannitol + NAD(P)+
-
686764
Pseudomonas fluorescens
D-fructose + NAD(P)H + H+
-
-
-
r
D-mannitol + NAD+
wild-type enzyme
686764
Pseudomonas fluorescens
D-fructose + NADH + H+
-
-
-
r
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at, both reaction directions
Pseudomonas fluorescens
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3
-
NAD(P)H
wild-type
Pseudomonas fluorescens
4.6
-
NADH
mutant D69A/D69A
Pseudomonas fluorescens
12
-
NAD(P)H
mutant D69A/D69A
Pseudomonas fluorescens
15
-
NADH
mutant D69A
Pseudomonas fluorescens
24
-
NAD(P)H
mutant D69A
Pseudomonas fluorescens
26
-
NADH
wild-type
Pseudomonas fluorescens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at, both reaction directions
Pseudomonas fluorescens
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
; binding structure, the carboxylate group of Asp69 forms a bifurcated hydrogen bond with the 2' and 3' hydroxyl groups of the adenosine of NAD+ and contributes to the 400fold preference of the enzyme for NAD+ as compared to NADP+, overview
Pseudomonas fluorescens
NADH
-
Pseudomonas fluorescens
NADP+
400fold preference of the enzyme for NAD+ as compared to NADP+
Pseudomonas fluorescens
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
no activation of M2DH by bovine serum albumin
Pseudomonas fluorescens
Application (protein specific)
Application
Commentary
Organism
industry
redox balancing between the intracellular NADP(H) and NAD(H) based on NAD(P)(H)-dependent interconversion of mannitol and fructose by M2DH may be a useful strategy of metabolic engineering
Pseudomonas fluorescens
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli; expression of wild-type and mutant enzymes in Escherichia coli strain JM109
Pseudomonas fluorescens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
; binding structure, the carboxylate group of Asp69 forms a bifurcated hydrogen bond with the 2' and 3' hydroxyl groups of the adenosine of NAD+ and contributes to the 400fold preference of the enzyme for NAD+ as compared to NADP+, overview
Pseudomonas fluorescens
NADH
-
Pseudomonas fluorescens
NADP+
400fold preference of the enzyme for NAD+ as compared to NADP+
Pseudomonas fluorescens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D69A
site-directed mutagenesis, the mutant shows an altered cofactor specificity compared to the wild-type enzyme, which is switched to NADP(H), EC 1.1.1.138, NADP(H) is equally utilized as NAD(H); utilizes NAD(H) and NADP(H) with similar catalytic efficiencies. Uses NADP(H) almost as well as wild-type enzyme uses NAD(H)
Pseudomonas fluorescens
E68K
site-directed mutagenesis, the mutant shows an altered cofactor specificity compared to the wild-type enzyme, which is switched to NADP(H), EC 1.1.1.138, NADP(H) is preferred by 10fold over NAD(H)
Pseudomonas fluorescens
E68K/D69A
shows about a 10fold preference for NADP(H) over NAD(H), accompanied by a small decrease in catalytic efficiency for NAD(H)-dependent reactions as compared to wild-type enzyme
Pseudomonas fluorescens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
no inhibition of M2DH by bovine serum albumin
Pseudomonas fluorescens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetic analysis, recombinant wild-type and mutant enzymes, overview
Pseudomonas fluorescens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-mannitol + NAD+
Pseudomonas fluorescens
wild-type enzyme
D-fructose + NADH + H+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
mutants purified to apparent homogeneity
Pseudomonas fluorescens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-mannitol + NAD(P)+
-
686764
Pseudomonas fluorescens
D-fructose + NAD(P)H + H+
-
-
-
r
D-mannitol + NAD+
wild-type enzyme
686764
Pseudomonas fluorescens
D-fructose + NADH + H+
-
-
-
r
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at, both reaction directions
Pseudomonas fluorescens
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3
-
NAD(P)H
wild-type
Pseudomonas fluorescens
4.6
-
NADH
mutant D69A/D69A
Pseudomonas fluorescens
12
-
NAD(P)H
mutant D69A/D69A
Pseudomonas fluorescens
15
-
NADH
mutant D69A
Pseudomonas fluorescens
24
-
NAD(P)H
mutant D69A
Pseudomonas fluorescens
26
-
NADH
wild-type
Pseudomonas fluorescens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at, both reaction directions
Pseudomonas fluorescens
Other publictions for EC 1.1.1.67
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)
737257
Jordan
Hxt13, Hxt15, Hxt16 and Hxt17 ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae EBY.VW4000
Sci. Rep.
6
0000
2016
-
-
-
-
-
-
-
2
-
-
-
16
-
12
-
-
-
-
-
-
-
-
19
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
16
-
-
-
-
-
-
-
-
19
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
725508
Klimacek
Dynamic mechanism of proton tr ...
Pseudomonas fluorescens
J. Biol. Chem.
287
6655-6667
2012
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722234
Krahulec
Enzymes of mannitol metabolism ...
Aspergillus fumigatus
FEBS J.
278
1264-1276
2011
-
-
-
-
-
-
2
7
-
-
-
2
-
2
-
-
-
1
-
-
-
-
7
-
-
-
2
5
-
-
-
3
4
-
-
-
-
-
3
-
-
-
-
2
4
7
-
-
-
2
-
-
-
-
-
-
-
-
7
-
-
-
2
5
-
-
-
-
-
-
-
-
6
6
711136
Klimacek
The oxyanion hole of Pseudomon ...
Pseudomonas fluorescens
Biochem. J.
425
455-463
2010
-
-
-
-
3
-
-
16
-
-
-
-
-
2
-
-
-
1
-
-
-
-
2
-
-
-
-
8
-
-
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-
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-
-
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-
-
3
-
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-
16
-
-
-
-
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-
-
-
-
-
-
2
-
-
-
-
8
-
-
-
-
-
-
-
-
16
16
712470
Klimacek
From alcohol dehydrogenase to ...
Pseudomonas fluorescens
J. Biol. Chem.
285
30644-30653
2010
-
-
1
-
3
-
2
22
-
-
1
-
-
2
-
-
-
-
-
-
-
-
2
1
-
-
-
11
-
-
-
2
6
-
-
-
-
1
2
-
3
-
-
2
6
22
-
-
1
-
-
-
-
-
-
-
-
-
2
1
-
-
-
11
-
-
-
-
-
-
-
-
21
21
697276
Krahulec
Polyol-specific long-chain deh ...
Aspergillus fumigatus
Chem. Biol. Interact.
178
274-282
2009
-
-
1
-
-
-
-
4
-
1
1
-
-
5
-
-
1
-
-
-
2
-
2
1
-
-
-
-
-
1
-
2
-
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-
-
1
2
-
-
-
-
-
-
4
-
1
1
-
-
-
-
1
-
-
2
-
2
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
686764
Bubner
Structure-guided engineering o ...
Pseudomonas fluorescens
FEBS Lett.
582
233-237
2008
1
1
1
-
3
-
1
1
-
-
-
1
-
2
-
-
1
-
-
-
-
-
2
-
1
-
-
6
1
-
-
3
-
-
-
1
1
1
3
-
3
-
-
1
-
1
-
-
-
1
-
-
-
1
-
-
-
-
2
-
1
-
-
6
1
-
-
-
-
-
-
-
-
-
695814
Song
Thermotoga maritima TM0298 is ...
Lactobacillus reuteri, Thermotoga maritima
Appl. Microbiol. Biotechnol.
81
485-495
2008
-
-
2
-
-
-
2
9
-
4
4
-
-
5
-
-
1
-
-
-
1
-
11
4
2
2
2
-
3
-
1
4
1
-
-
-
-
2
4
-
-
-
-
2
1
9
-
4
4
-
-
-
-
1
-
-
1
-
11
4
2
2
2
-
3
-
1
-
-
-
-
-
-
-
700553
Haghighatian
Isomalt production by cloning, ...
Pseudomonas fluorescens
Pak. J. Biol. Sci.
11
2001-2006
2008
-
1
1
-
-
-
-
-
-
-
1
-
-
3
-
-
1
-
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-
1
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5
1
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1
1
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1
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1
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-
1
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684173
Puttick
Crystallization, preliminary X ...
Thermotoga maritima
Acta Crystallogr. Sect. F
63
350-352
2007
-
-
1
1
-
-
-
-
-
-
-
-
-
1
-
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1
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-
-
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1
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1
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1
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-
685726
Baeumchen
D-mannitol production by resti ...
Leuconostoc pseudomesenteroides, Leuconostoc pseudomesenteroides ATCC12291
Biotechnol. J.
2
1408-1416
2007
-
1
1
-
1
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1
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2
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2
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1
1
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1
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1
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2
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668450
Watanabe
-
Overexpression of Saccharomyce ...
Saccharomyces cerevisiae
Enzyme Microb. Technol.
39
654-659
2006
-
-
-
-
-
-
-
-
-
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1
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1
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1
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1
-
1
-
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-
-
-
2
-
-
-
-
-
-
-
-
-
667238
Liu
Cloning, expression, purificat ...
Lactobacillus brevis
Appl. Biochem. Biotechnol.
121-124
391-401
2005
-
-
1
-
-
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1
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5
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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
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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667367
Parmentier
-
Enzymatic production of D-mann ...
Leuconostoc pseudomesenteroides
Biocatal. Biotransform.
23
1-7
2005
-
-
-
-
-
-
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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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2
1
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2
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2
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1
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2
-
2
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1
-
2
1
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-
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-
-
-
668058
Parmentier
Gluconobacter oxydans NAD-depe ...
Gluconobacter oxydans, Gluconobacter oxydans LMG 1489
Biotechnol. Lett.
27
305-311
2005
2
-
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2
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2
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2
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1
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1
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2
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2
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1
-
1
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-
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-
654309
Kaup
Metabolic engineering of Esche ...
Leuconostoc pseudomesenteroides
Appl. Microbiol. Biotechnol.
64
333-339
2004
-
1
1
-
-
-
-
-
-
-
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1
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1
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1
1
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1
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-
-
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-
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-
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-
654390
Hahn
A zinc-containing mannitol-2-d ...
Leuconostoc pseudomesenteroides
Arch. Microbiol.
179
101-107
2003
-
-
1
-
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1
3
2
-
1
2
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4
-
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1
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1
1
3
1
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2
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3
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1
3
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1
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3
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2
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1
2
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1
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1
1
3
1
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2
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654531
Klimacek
On the role of Bronsted cataly ...
Pseudomonas fluorescens
Biochem. J.
375
141-149
2003
-
-
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2
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-
-
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2
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1
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655223
Kavanagh
Crystal structure of Pseudomon ...
Pseudomonas fluorescens
Chem. Biol. Interact.
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551-558
2003
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655244
Graefe
Sensitive and specific photome ...
Leuconostoc mesenteroides
Clin. Chem. Lab. Med.
41
1049-1055
2003
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Korakli
Purification and characterisat ...
Lactobacillus sanfranciscensis
FEMS Microbiol. Lett.
220
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654295
Aarnikunnas
The mannitol dehydrogenase gen ...
Leuconostoc mesenteroides, Leuconostoc mesenteroides ATCC-9135
Appl. Microbiol. Biotechnol.
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2002
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654504
Klimacek
A catalytic consensus motif fo ...
Pseudomonas fluorescens
Biochem. J.
367
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2002
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656092
Kavanagh
Crystal structure of Pseudomon ...
Pseudomonas fluorescens
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667571
Klimacek
Examining the relative timing ...
Pseudomonas fluorescens
Biochemistry
41
10158-10165
2002
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287261
Slatner
Kinetic study of the catalytic ...
Pseudomonas fluorescens
Biochemistry
38
10489-10498
1999
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2
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287260
Slatner
Enzymic synthesis of mannitol: ...
Pseudomonas fluorescens
Ann. N. Y. Acad. Sci.
864
450-453
1998
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287259
Schafer
Mannitol dehydrogenase from Rh ...
Rhodobacter sphaeroides
Appl. Microbiol. Biotechnol.
48
47-52
1997
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287262
Brunker
Cloning, nucleotide sequence a ...
Pseudomonas fluorescens
Biochim. Biophys. Acta
1351
157-167
1997
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94720
Schmatz D.M.; Baginsky W.F.; Turner
Evidence for and characterizat ...
Eimeria tenella
Mol. Biochem. Parasitol.
32
263-270
1989
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1
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287237
Schneider
Purification and properties of ...
Rhodobacter sphaeroides
Eur. J. Biochem.
184
15-19
1989
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6
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1
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287238
Quain
Growth and metabolism of manni ...
Saccharomyces cerevisiae
J. Gen. Microbiol.
133
1675-1684
1987
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287239
Richter
D-Mannitol dehydrogenase and D ...
Tetraselmis subcordiformis
Planta
170
528-534
1987
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2
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287240
Mori
Pyruvate formation and sugar m ...
Brevibacterium flavum, Brevibacterium flavum 2247
Agric. Biol. Chem.
51
129-138
1987
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4
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4
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287241
Kulbe
-
Anwendung von Membranverfahren ...
Saccharomyces cerevisiae
GBF Monogr.
9
189-200
1986
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5
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1
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287242
Mathis
Characterization of a mannitol ...
Bradyrhizobium japonicum
Appl. Environ. Microbiol.
52
81-85
1986
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287243
Davis
Maintenance of different manni ...
Pseudomonas sp.
Appl. Environ. Microbiol.
50
743-748
1985
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287244
Allenza
Enzymes related to fructose ut ...
Burkholderia cepacia
J. Bacteriol.
150
1348-1356
1982
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94717
Hult
The distribution of the NADPH ...
Fomes pinicola
Arch. Microbiol.
128
253-255
1980
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287246
Mulongoy
-
Some effects of mannitol on th ...
Bradyrhizobium japonicum
Curr. Microbiol.
1
335-340
1978
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3
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287247
Yamanaka
-
Physicochemical properties of ...
Leuconostoc mesenteroides
Agric. Biol. Chem.
41
1695-1699
1977
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1
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1
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1
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287248
Mehta
Mannitol oxidation in two Micr ...
Actinoplanes missouriensis, Gluconobacter oxydans, Lactobacillus brevis, Mycobacterium smegmatis, Nocardia erythropolis, Sinorhizobium meliloti, Streptomyces lavendulae
Appl. Environ. Microbiol.
33
1013-1015
1977
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7
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7
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14
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14
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14
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7
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14
-
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287249
Kuykendall
Some features of mannitol meta ...
Bradyrhizobium japonicum
J. Gen. Microbiol.
98
291-295
1977
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5
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287250
Ueng
D-Mannitol dehydrogenase from ...
Absidia glauca
Biochemistry
16
107-111
1977
-
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1
4
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1
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1
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1
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2
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1
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287251
Ueng
D-Mannitol dehydrogenase from ...
Absidia glauca
Biochemistry
15
1743-1749
1976
-
-
-
-
-
-
2
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2
1
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2
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1
-
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1
1
3
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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2
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2
1
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1
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1
1
3
1
-
-
1
-
2
1
-
-
-
-
-
-
-
-
287252
Yamanaka
D-Mannitol dehydrogenase from ...
Lactobacillus brevis, Lactobacillus gayonii, Lactobacillus pentoaceticus, Leuconostoc mesenteroides
Methods Enzymol.
41B
138-142
1975
-
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1
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9
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1
4
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4
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1
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1
1
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8
-
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4
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2
8
-
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8
1
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9
-
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1
4
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1
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1
1
-
8
-
-
-
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-
4
-
2
-
-
-
-
-
-
-
285866
Sasajima
-
Polyol dehydrogenases in the s ...
Gluconobacter oxydans
Agric. Biol. Chem.
32
161-169
1968
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-
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3
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1
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1
1
2
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1
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2
2
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2
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2
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3
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1
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1
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1
1
2
-
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-
1
-
2
2
-
-
-
-
-
-
-
-
287253
Yamanaka
Production of polyol dehydroge ...
Lactobacillus brevis, Lactobacillus gayonii, Lactobacillus pentoaceticus, Leuconostoc mesenteroides, Pseudomonas aeruginosa, Pseudomonas coronafaciens, Pseudomonas fluorescens, Sarcina aurantiaca, Sarcina marginata
Can. J. Microbiol.
14
391-396
1968
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9
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9
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18
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18
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18
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9
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18
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287255
Sakai
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Leuconostoc mesenteroides, no activity in Lactobacillus plantarum
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1968
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1
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1
4
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1
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2
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3
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2
2
2
2
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2
1
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1
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4
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1
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3
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2
2
2
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287256
Sakai
Crystalline D-mannitol:NAD+ ox ...
Leuconostoc mesenteroides
Biochim. Biophys. Acta
151
684-686
1968
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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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2
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2
1
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1
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1
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1
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2
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287257
Horecker
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Mannitol dehydrogenase (crysta ...
Lactobacillus brevis
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143-146
1966
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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
2
2
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2
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1
2
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2
1
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1
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1
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1
2
2
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2
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1
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287258
Martinez
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A specific mannitol dehydrogen ...
Lactobacillus brevis
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1598-1603
1963
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4
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1
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1
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1
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2
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2
2
1
2
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2
1
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4
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1
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1
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2
2
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2
2
1
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