BRENDA - Enzyme Database show
show all sequences of 1.1.1.179

Structure of monkey dimeric dihydrodiol dehydrogenase in complex with isoascorbic acid

Carbone, V.; Sumii, R.; Ishikura, S.; Asada, Y.; Hara, A.; El-Kabbani, O.; Acta Crystallogr. Sect. D 64, 532-542 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
wild-type protein and mutants are expressed in Escherichia coli BL21 (DE3)
Macaca fascicularis
Crystallization (Commentary)
Crystallization
Organism
crystals are obtained at 19.9C in a culture plate via the vapour-diffusion method, crystal structure of dimeric D-xylose dehydrogenase complexed with the inhibitor isoascorbic acid is determined at 2.59 A resolution
Macaca fascicularis
Engineering
Amino acid exchange
Commentary
Organism
A36D
site-directed mutagenesis
Macaca fascicularis
D280A
by site-directed mutagenesis
Macaca fascicularis
F154A
by site-directed mutagenesis
Macaca fascicularis
F279A
by site-directed mutagenesis
Macaca fascicularis
H76Q
by site-directed mutagenesis
Macaca fascicularis
H79Q
by site-directed mutagenesis
Macaca fascicularis
K97M
by site-directed mutagenesis
Macaca fascicularis
K97R
by site-directed mutagenesis
Macaca fascicularis
R37A
site-directed mutagenesis
Macaca fascicularis
R37D
site-directed mutagenesis
Macaca fascicularis
R41A
by site-directed mutagenesis
Macaca fascicularis
R41D
by site-directed mutagenesis
Macaca fascicularis
W125Y
by site-directed mutagenesis
Macaca fascicularis
W254A
by site-directed mutagenesis
Macaca fascicularis
W254Y
by site-directed mutagenesis
Macaca fascicularis
Inhibitors
Inhibitors
Commentary
Organism
Structure
4-hydroxyacetophenone
-
Macaca fascicularis
isoascorbic acid
competitive inhibitor
Macaca fascicularis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.4
-
D-xylose
oxidation reaction of mutant R41A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
2.9
-
D-xylose
oxidation reaction of mutant R41D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
3.4
-
D-xylose
oxidation reaction of mutant R37A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
4.4
-
D-xylose
oxidation reaction of wild type enzyme, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
8
9
D-xylose
oxidation reaction of mutant F279A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
11
-
D-xylose
oxidation reaction of mutante R37D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
14
-
D-xylose
oxidation reaction of mutant W254Y, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
15
-
D-xylose
oxidation reaction of mutant H79Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
36
-
D-xylose
oxidation reaction of mutant F154A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
41
-
D-xylose
oxidation reaction of mutant H76Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
65
-
D-xylose
oxidation reaction of mutant A36D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
67
-
D-xylose
oxidation reaction of mutant W125Y, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
90
-
D-xylose
oxidation reaction of mutant W254A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-xylose + NADP+
Macaca fascicularis
enzyme has dehydrogenase and reductase activities, enzyme is identical to dihydrodiol dehydrogenase
D-xylono-1,5-lactone + NADPH + H+
-
-
?
additional information
Macaca fascicularis
D-xylose dehydrogenase catalyzes the NADP+-linked oxidation of dihydrodiols of aromatic hydrocarbons to their corresponding catechols and is regarded as a toxication enzyme in the metabolism of carcinogenic polycyclic aromatic hydrocarbons because oxidation by the enzyme yields reactive and redox-active ortho-quinones and reactive oxygen species, broad substrate specificity indicates additional roles of the enzyme in the metabolism of endogenous and xenobiotic carbonyl compounds and the prevention of the development of glycation
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Macaca fascicularis
Q9TQS6
-
-
Purification (Commentary)
Commentary
Organism
the recombinant enzymes are purified from the 12000g supernatants of the homogenates of the cells
Macaca fascicularis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-xylose + NADP+
enzyme has dehydrogenase and reductase activities, enzyme is identical to dihydrodiol dehydrogenase
684150
Macaca fascicularis
D-xylono-1,5-lactone + NADPH + H+
-
-
-
?
additional information
D-xylose dehydrogenase catalyzes the NADP+-linked oxidation of dihydrodiols of aromatic hydrocarbons to their corresponding catechols and is regarded as a toxication enzyme in the metabolism of carcinogenic polycyclic aromatic hydrocarbons because oxidation by the enzyme yields reactive and redox-active ortho-quinones and reactive oxygen species, broad substrate specificity indicates additional roles of the enzyme in the metabolism of endogenous and xenobiotic carbonyl compounds and the prevention of the development of glycation
684150
Macaca fascicularis
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
-
Macaca fascicularis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.4
-
D-xylose
oxidation reaction of mutant R37D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
0.45
-
D-xylose
oxidation reaction of mutant A36D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
0.5
-
D-xylose
oxidation reaction of mutant H76Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
0.9
-
D-xylose
oxidation reaction of mutant H79Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
1
-
D-xylose
oxidation reaction of mutant R41D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
1.2
-
D-xylose
oxidation reaction of mutant R37A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
1.7
-
D-xylose
oxidation reaction of mutant R41A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
2.6
-
D-xylose
oxidation reaction of wild type enzyme, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Macaca fascicularis
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Macaca fascicularis
Cloned(Commentary) (protein specific)
Commentary
Organism
wild-type protein and mutants are expressed in Escherichia coli BL21 (DE3)
Macaca fascicularis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Macaca fascicularis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystals are obtained at 19.9C in a culture plate via the vapour-diffusion method, crystal structure of dimeric D-xylose dehydrogenase complexed with the inhibitor isoascorbic acid is determined at 2.59 A resolution
Macaca fascicularis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
A36D
site-directed mutagenesis
Macaca fascicularis
D280A
by site-directed mutagenesis
Macaca fascicularis
F154A
by site-directed mutagenesis
Macaca fascicularis
F279A
by site-directed mutagenesis
Macaca fascicularis
H76Q
by site-directed mutagenesis
Macaca fascicularis
H79Q
by site-directed mutagenesis
Macaca fascicularis
K97M
by site-directed mutagenesis
Macaca fascicularis
K97R
by site-directed mutagenesis
Macaca fascicularis
R37A
site-directed mutagenesis
Macaca fascicularis
R37D
site-directed mutagenesis
Macaca fascicularis
R41A
by site-directed mutagenesis
Macaca fascicularis
R41D
by site-directed mutagenesis
Macaca fascicularis
W125Y
by site-directed mutagenesis
Macaca fascicularis
W254A
by site-directed mutagenesis
Macaca fascicularis
W254Y
by site-directed mutagenesis
Macaca fascicularis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
4-hydroxyacetophenone
-
Macaca fascicularis
isoascorbic acid
competitive inhibitor
Macaca fascicularis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.4
-
D-xylose
oxidation reaction of mutant R41A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
2.9
-
D-xylose
oxidation reaction of mutant R41D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
3.4
-
D-xylose
oxidation reaction of mutant R37A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
4.4
-
D-xylose
oxidation reaction of wild type enzyme, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
8
9
D-xylose
oxidation reaction of mutant F279A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
11
-
D-xylose
oxidation reaction of mutante R37D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
14
-
D-xylose
oxidation reaction of mutant W254Y, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
15
-
D-xylose
oxidation reaction of mutant H79Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
36
-
D-xylose
oxidation reaction of mutant F154A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
41
-
D-xylose
oxidation reaction of mutant H76Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
65
-
D-xylose
oxidation reaction of mutant A36D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
67
-
D-xylose
oxidation reaction of mutant W125Y, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
90
-
D-xylose
oxidation reaction of mutant W254A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
Macaca fascicularis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-xylose + NADP+
Macaca fascicularis
enzyme has dehydrogenase and reductase activities, enzyme is identical to dihydrodiol dehydrogenase
D-xylono-1,5-lactone + NADPH + H+
-
-
?
additional information
Macaca fascicularis
D-xylose dehydrogenase catalyzes the NADP+-linked oxidation of dihydrodiols of aromatic hydrocarbons to their corresponding catechols and is regarded as a toxication enzyme in the metabolism of carcinogenic polycyclic aromatic hydrocarbons because oxidation by the enzyme yields reactive and redox-active ortho-quinones and reactive oxygen species, broad substrate specificity indicates additional roles of the enzyme in the metabolism of endogenous and xenobiotic carbonyl compounds and the prevention of the development of glycation
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
the recombinant enzymes are purified from the 12000g supernatants of the homogenates of the cells
Macaca fascicularis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-xylose + NADP+
enzyme has dehydrogenase and reductase activities, enzyme is identical to dihydrodiol dehydrogenase
684150
Macaca fascicularis
D-xylono-1,5-lactone + NADPH + H+
-
-
-
?
additional information
D-xylose dehydrogenase catalyzes the NADP+-linked oxidation of dihydrodiols of aromatic hydrocarbons to their corresponding catechols and is regarded as a toxication enzyme in the metabolism of carcinogenic polycyclic aromatic hydrocarbons because oxidation by the enzyme yields reactive and redox-active ortho-quinones and reactive oxygen species, broad substrate specificity indicates additional roles of the enzyme in the metabolism of endogenous and xenobiotic carbonyl compounds and the prevention of the development of glycation
684150
Macaca fascicularis
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
-
Macaca fascicularis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.4
-
D-xylose
oxidation reaction of mutant R37D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
0.45
-
D-xylose
oxidation reaction of mutant A36D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
0.5
-
D-xylose
oxidation reaction of mutant H76Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
0.9
-
D-xylose
oxidation reaction of mutant H79Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
1
-
D-xylose
oxidation reaction of mutant R41D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
1.2
-
D-xylose
oxidation reaction of mutant R37A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
1.7
-
D-xylose
oxidation reaction of mutant R41A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
2.6
-
D-xylose
oxidation reaction of wild type enzyme, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
Macaca fascicularis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Macaca fascicularis
Other publictions for EC 1.1.1.179
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)
723749
Mihasan
Evidence of a plasmid-encoded ...
Paenarthrobacter nicotinovorans
Res. Microbiol.
164
22-30
2013
-
-
1
-
-
-
-
3
-
1
1
-
-
1
-
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-
-
-
-
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3
1
-
-
-
3
-
-
-
2
-
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-
-
1
2
-
-
-
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-
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3
-
1
1
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-
-
-
-
-
-
-
3
1
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-
3
-
-
-
-
-
-
-
-
3
3
724150
Ahmed
-
Oxidation and reduction of D-x ...
Ogataea angusta
Aust. J. Basic Appl. Sci.
5
95-100
2011
-
-
-
-
-
-
-
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2
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1
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3
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2
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2
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2
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3
-
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-
-
-
-
-
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-
725867
Nygard
Bioconversion of d-xylose to d ...
Trichoderma reesei
Metab. Eng.
13
383-391
2011
-
1
1
-
-
-
-
-
-
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-
1
-
1
-
-
-
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1
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1
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1
1
1
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1
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1
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-
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-
-
-
-
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-
698940
Johnsen
D-xylose degradation pathway i ...
Haloferax volcanii, Haloferax volcanii DS2, Haloferax volcanii GR501
J. Biol. Chem.
284
27290-27303
2009
1
-
1
-
1
-
-
6
-
-
3
2
-
4
-
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1
-
-
1
3
-
12
1
-
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2
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1
-
2
2
-
1
-
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6
-
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3
2
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-
1
-
1
3
-
12
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684150
Carbone
Structure of monkey dimeric di ...
Macaca fascicularis
Acta Crystallogr. Sect. D
64
532-542
2008
-
-
1
1
15
-
2
13
-
-
-
2
-
2
-
-
1
-
-
-
-
-
2
1
-
-
-
8
1
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-
1
-
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-
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-
1
1
1
15
-
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2
-
13
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2
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1
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2
1
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8
1
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-
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-
686797
Berghaell
Identification in the mould Hy ...
Trichoderma reesei
FEMS Microbiol. Lett.
277
249-253
2007
-
-
1
-
-
-
-
4
-
1
1
1
-
1
-
-
1
-
-
-
1
-
6
1
1
-
-
2
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
4
-
1
1
1
-
-
-
1
-
-
1
-
6
1
1
-
-
2
1
-
-
-
-
-
-
-
-
-
655884
Johnsen
Novel xylose dehydrogenase in ...
Haloarcula marismortui
J. Bacteriol.
186
6198-6207
2004
-
-
1
-
-
-
-
3
-
3
2
1
-
1
-
-
1
-
-
1
1
-
5
1
2
1
-
3
1
1
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
3
-
3
2
1
-
-
-
1
-
1
1
-
5
1
2
1
-
3
1
1
-
-
-
-
-
-
3
3
286128
Aoki
Identity of dimeric dihydrodio ...
Canis lupus familiaris, Homo sapiens, Macaca fuscata, Oryctolagus cuniculus, Sus scrofa
Chem. Biol. Interact.
130-132
775-784
2001
4
-
-
-
2
-
1
4
-
-
-
5
-
10
-
-
4
1
-
8
2
-
18
-
-
-
-
-
8
-
-
7
-
-
-
4
-
-
7
-
2
-
-
1
-
4
-
-
-
5
-
-
-
4
-
8
2
-
18
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
286127
Asada
Roles of His-79 and Tyr-180 of ...
Macaca fuscata
Biochem. Biophys. Res. Commun.
278
333-337
2000
1
-
1
-
2
-
1
9
-
-
2
-
-
1
-
-
1
-
-
1
3
-
3
1
-
-
-
-
-
-
-
1
-
-
-
1
-
1
1
-
2
-
-
1
-
9
-
-
2
-
-
-
-
1
-
1
3
-
3
1
-
-
-
-
-
-
-
-
-
-
-
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Zepeda
NADP(+)-dependent D-xylose deh ...
Sus scrofa
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1990
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2
9
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2
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1
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1
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1
1
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7
1
1
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7
1
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2
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9
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1
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7
1
1
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7
1
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286124
Wissler
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Bos taurus, Canis lupus familiaris, Sus scrofa
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1300-1301
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3
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3
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7
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24
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3
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3
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3
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7
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24
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286125
Suzuki
Oxidation and reduction of D-x ...
Starmera quercuum
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1973
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1
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1
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