BRENDA - Enzyme Database show
show all sequences of 1.1.1.10

Identification of amino acid residues involved in substrate recognition of L-xylulose reductase by site-directed mutagenesis

Ishikura, S.; Isaji, T.; Usami, N.; Nakagawa, J.; El-Kabbani, O.; Hara, A.; Chem. Biol. Interact. 143-144, 543-550 (2003)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of wild-type and mutant enzymes in Escherichia coli
Rattus norvegicus
Engineering
Amino acid exchange
Commentary
Organism
H146L
site-directed mutagenesis, altered activity
Rattus norvegicus
K153M
site-directed mutagenesis, active site mutant, complete loss of activity
Rattus norvegicus
L143F
site-directed mutagenesis, altered activity
Rattus norvegicus
N190V
site-directed mutagenesis, altered activity
Rattus norvegicus
N190V/W191S
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity
Rattus norvegicus
N190V/W191S/Q137M/L143F/H146L
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows high 3-ketosteroid reductase activity
Rattus norvegicus
Q137M
site-directed mutagenesis, altered activity, stable against cold inactivation
Rattus norvegicus
Q137M/F241L
site-directed mutagenesis, altered activity, sensitive to cold inactivation like the wild-type enzyme
Rattus norvegicus
Q137M/L143F
site-directed mutagenesis, increased Km for L-xylulose compared to the wild-type
Rattus norvegicus
Q137M/L143F/H146L
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows 3-ketosteroid reductase activity
Rattus norvegicus
S136A
site-directed mutagenesis, active site mutant, complete loss of activity
Rattus norvegicus
W191F
site-directed mutagenesis, altered activity
Rattus norvegicus
W191S
site-directed mutagenesis, altered activity
Rattus norvegicus
Y149F
site-directed mutagenesis, active site mutant, complete loss of activity
Rattus norvegicus
Inhibitors
Inhibitors
Commentary
Organism
Structure
n-butyric acid
specific, binds to the enzyme-NADP+ complex, the mutant enzymes show altered sensitivity to inhibition, overview
Rattus norvegicus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00067
-
NADP+
pH 7.0, 25C, mutant S136A
Rattus norvegicus
0.0013
-
NADP+
pH 7.0, 25C, mutant Y149F
Rattus norvegicus
0.002
-
NADPH
pH 7.0, 25C, mutant Y149F
Rattus norvegicus
0.003
-
NADP+
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
0.0046
-
NADPH
pH 7.0, 25C, mutant S136A
Rattus norvegicus
0.005
-
1,4-dibromo-2,3-butanedione
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
0.007
-
NADPH
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
0.0099
-
L-xylitol
pH 7.0, 25C, mutant Y149F
Rattus norvegicus
0.011
-
L-xylitol
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
0.013
-
L-xylitol
pH 7.0, 25C, mutant S136A
Rattus norvegicus
0.05
-
1,4-dibromo-2,3-butanedione
pH 7.0, 25C, mutant S136A
Rattus norvegicus
0.053
-
NADPH
pH 7.0, 25C, mutant K153M
Rattus norvegicus
0.085
-
L-xylitol
pH 7.0, 25C, mutant K153M
Rattus norvegicus
0.092
-
L-xylulose
pH 7.0, 25C, mutant H146L
Rattus norvegicus
0.1
-
1,4-dibromo-2,3-butanedione
pH 7.0, 25C, mutant K153M
Rattus norvegicus
0.117
-
NADP+
pH 7.0, 25C, mutant K153M
Rattus norvegicus
0.139
-
1,4-dibromo-2,3-butanedione
pH 7.0, 25C, mutant Y149F
Rattus norvegicus
0.14
-
L-xylulose
pH 7.0, 25C, wild-type enzyme and mutant L143F
Rattus norvegicus
0.31
-
L-xylulose
pH 7.0, 25C, mutant N190V
Rattus norvegicus
0.33
-
L-xylulose
pH 7.0, 25C, mutant Q137M
Rattus norvegicus
0.78
-
diacetyl
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
1.2
-
diacetyl
pH 7.0, 25C, mutant H146L
Rattus norvegicus
2.6
-
diacetyl
pH 7.0, 25C, mutant N190V
Rattus norvegicus
2.7
-
diacetyl
pH 7.0, 25C, mutant N190V/W191S/Q137M/L143F/H146L
Rattus norvegicus
3
-
diacetyl
pH 7.0, 25C, mutant Q137M
Rattus norvegicus
3.6
-
L-xylulose
pH 7.0, 25C, mutant Q137M/L143F
Rattus norvegicus
5.2
-
diacetyl
pH 7.0, 25C, mutant W191F
Rattus norvegicus
6.2
-
diacetyl
pH 7.0, 25C, mutant L143F
Rattus norvegicus
7.2
-
L-xylulose
pH 7.0, 25C, mutant W191F
Rattus norvegicus
9.6
-
diacetyl
pH 7.0, 25C, mutant Q137M/L143F/H146L
Rattus norvegicus
11
-
diacetyl
pH 7.0, 25C, mutant Q137M/L143F
Rattus norvegicus
16
-
diacetyl
pH 7.0, 25C, mutant N190V/W191S
Rattus norvegicus
42
-
diacetyl
pH 7.0, 25C, mutant W191S
Rattus norvegicus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Rattus norvegicus
16020
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26500
-
x * 26500
Rattus norvegicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
diacetyl + NAD(P)H
Rattus norvegicus
detoxification of alpha-dicarbonyl compounds
acetoin + NAD(P)+
-
-
r
L-xylulose + NADPH + H+
Rattus norvegicus
part of the uronate cycle, involved in osmoregulation in the kidney
L-xylitol + NADP+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
-
-
-
Reaction
Reaction
Commentary
Organism
xylitol + NADP+ = L-xylulose + NADPH + H+
enzyme with dual function showing L-xylulose reductase and dicarbonyl reductase activities, it is probably identical with sperm 34 kDa protein P34H and diacetyl reductase, EC 1.1.1.5, the amino acid residues Ser136, Tyr149, and Lys153 form the catalytic triad
Rattus norvegicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
brush border
Rattus norvegicus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,4-dibromo-2,3-butanedione + NADPH
dicarbonyl reductase activity
655222
Rattus norvegicus
? + NADP+
-
-
-
r
diacetyl + NAD(P)H
detoxification of alpha-dicarbonyl compounds
655222
Rattus norvegicus
acetoin + NAD(P)+
-
-
-
r
diacetyl + NAD(P)H
dicarbonyl reductase activity
655222
Rattus norvegicus
acetoin + NAD(P)+
-
-
-
r
L-xylulose + NADPH + H+
part of the uronate cycle, involved in osmoregulation in the kidney
655222
Rattus norvegicus
L-xylitol + NADP+
-
-
-
r
L-xylulose + NADPH + H+
L-xylulose reductase activity
655222
Rattus norvegicus
L-xylitol + NADP+
-
-
-
r
additional information
the size and hydrophobicity of the amino acid residues involved in substrate recognition, i.e. Q137, L143, H146, N190, and W191, is important, mutants N190V, N190V/W191S, Q137M/L143F/H146L, and N190V/W191S/Q137M/L143F/H146L show reductive activity with 4-nitroacetophenone, 5beta-androstane-3,17-dione, 5beta-androstan-17beta-ol-3-one, and 5beta-androstane-3alpha,17beta-diol, overview
655222
Rattus norvegicus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 26500
Rattus norvegicus
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Rattus norvegicus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0005
-
NADPH
pH 7.0, 25C, mutant K153M
Rattus norvegicus
0.0006
-
NADPH
pH 7.0, 25C, mutant S136A
Rattus norvegicus
0.0009
-
NADPH
pH 7.0, 25C, mutant Y149F
Rattus norvegicus
9.5
-
NADP+
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
25
-
NADPH
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Rattus norvegicus
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Rattus norvegicus
NADPH
-
Rattus norvegicus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of wild-type and mutant enzymes in Escherichia coli
Rattus norvegicus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Rattus norvegicus
NADPH
-
Rattus norvegicus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
H146L
site-directed mutagenesis, altered activity
Rattus norvegicus
K153M
site-directed mutagenesis, active site mutant, complete loss of activity
Rattus norvegicus
L143F
site-directed mutagenesis, altered activity
Rattus norvegicus
N190V
site-directed mutagenesis, altered activity
Rattus norvegicus
N190V/W191S
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity
Rattus norvegicus
N190V/W191S/Q137M/L143F/H146L
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows high 3-ketosteroid reductase activity
Rattus norvegicus
Q137M
site-directed mutagenesis, altered activity, stable against cold inactivation
Rattus norvegicus
Q137M/F241L
site-directed mutagenesis, altered activity, sensitive to cold inactivation like the wild-type enzyme
Rattus norvegicus
Q137M/L143F
site-directed mutagenesis, increased Km for L-xylulose compared to the wild-type
Rattus norvegicus
Q137M/L143F/H146L
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows 3-ketosteroid reductase activity
Rattus norvegicus
S136A
site-directed mutagenesis, active site mutant, complete loss of activity
Rattus norvegicus
W191F
site-directed mutagenesis, altered activity
Rattus norvegicus
W191S
site-directed mutagenesis, altered activity
Rattus norvegicus
Y149F
site-directed mutagenesis, active site mutant, complete loss of activity
Rattus norvegicus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
n-butyric acid
specific, binds to the enzyme-NADP+ complex, the mutant enzymes show altered sensitivity to inhibition, overview
Rattus norvegicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00067
-
NADP+
pH 7.0, 25C, mutant S136A
Rattus norvegicus
0.0013
-
NADP+
pH 7.0, 25C, mutant Y149F
Rattus norvegicus
0.002
-
NADPH
pH 7.0, 25C, mutant Y149F
Rattus norvegicus
0.003
-
NADP+
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
0.0046
-
NADPH
pH 7.0, 25C, mutant S136A
Rattus norvegicus
0.005
-
1,4-dibromo-2,3-butanedione
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
0.007
-
NADPH
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
0.0099
-
L-xylitol
pH 7.0, 25C, mutant Y149F
Rattus norvegicus
0.011
-
L-xylitol
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
0.013
-
L-xylitol
pH 7.0, 25C, mutant S136A
Rattus norvegicus
0.05
-
1,4-dibromo-2,3-butanedione
pH 7.0, 25C, mutant S136A
Rattus norvegicus
0.053
-
NADPH
pH 7.0, 25C, mutant K153M
Rattus norvegicus
0.085
-
L-xylitol
pH 7.0, 25C, mutant K153M
Rattus norvegicus
0.092
-
L-xylulose
pH 7.0, 25C, mutant H146L
Rattus norvegicus
0.1
-
1,4-dibromo-2,3-butanedione
pH 7.0, 25C, mutant K153M
Rattus norvegicus
0.117
-
NADP+
pH 7.0, 25C, mutant K153M
Rattus norvegicus
0.139
-
1,4-dibromo-2,3-butanedione
pH 7.0, 25C, mutant Y149F
Rattus norvegicus
0.14
-
L-xylulose
pH 7.0, 25C, wild-type enzyme and mutant L143F
Rattus norvegicus
0.31
-
L-xylulose
pH 7.0, 25C, mutant N190V
Rattus norvegicus
0.33
-
L-xylulose
pH 7.0, 25C, mutant Q137M
Rattus norvegicus
0.78
-
diacetyl
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
1.2
-
diacetyl
pH 7.0, 25C, mutant H146L
Rattus norvegicus
2.6
-
diacetyl
pH 7.0, 25C, mutant N190V
Rattus norvegicus
2.7
-
diacetyl
pH 7.0, 25C, mutant N190V/W191S/Q137M/L143F/H146L
Rattus norvegicus
3
-
diacetyl
pH 7.0, 25C, mutant Q137M
Rattus norvegicus
3.6
-
L-xylulose
pH 7.0, 25C, mutant Q137M/L143F
Rattus norvegicus
5.2
-
diacetyl
pH 7.0, 25C, mutant W191F
Rattus norvegicus
6.2
-
diacetyl
pH 7.0, 25C, mutant L143F
Rattus norvegicus
7.2
-
L-xylulose
pH 7.0, 25C, mutant W191F
Rattus norvegicus
9.6
-
diacetyl
pH 7.0, 25C, mutant Q137M/L143F/H146L
Rattus norvegicus
11
-
diacetyl
pH 7.0, 25C, mutant Q137M/L143F
Rattus norvegicus
16
-
diacetyl
pH 7.0, 25C, mutant N190V/W191S
Rattus norvegicus
42
-
diacetyl
pH 7.0, 25C, mutant W191S
Rattus norvegicus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Rattus norvegicus
16020
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26500
-
x * 26500
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
diacetyl + NAD(P)H
Rattus norvegicus
detoxification of alpha-dicarbonyl compounds
acetoin + NAD(P)+
-
-
r
L-xylulose + NADPH + H+
Rattus norvegicus
part of the uronate cycle, involved in osmoregulation in the kidney
L-xylitol + NADP+
-
-
r
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
brush border
Rattus norvegicus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,4-dibromo-2,3-butanedione + NADPH
dicarbonyl reductase activity
655222
Rattus norvegicus
? + NADP+
-
-
-
r
diacetyl + NAD(P)H
detoxification of alpha-dicarbonyl compounds
655222
Rattus norvegicus
acetoin + NAD(P)+
-
-
-
r
diacetyl + NAD(P)H
dicarbonyl reductase activity
655222
Rattus norvegicus
acetoin + NAD(P)+
-
-
-
r
L-xylulose + NADPH + H+
part of the uronate cycle, involved in osmoregulation in the kidney
655222
Rattus norvegicus
L-xylitol + NADP+
-
-
-
r
L-xylulose + NADPH + H+
L-xylulose reductase activity
655222
Rattus norvegicus
L-xylitol + NADP+
-
-
-
r
additional information
the size and hydrophobicity of the amino acid residues involved in substrate recognition, i.e. Q137, L143, H146, N190, and W191, is important, mutants N190V, N190V/W191S, Q137M/L143F/H146L, and N190V/W191S/Q137M/L143F/H146L show reductive activity with 4-nitroacetophenone, 5beta-androstane-3,17-dione, 5beta-androstan-17beta-ol-3-one, and 5beta-androstane-3alpha,17beta-diol, overview
655222
Rattus norvegicus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 26500
Rattus norvegicus
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Rattus norvegicus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0005
-
NADPH
pH 7.0, 25C, mutant K153M
Rattus norvegicus
0.0006
-
NADPH
pH 7.0, 25C, mutant S136A
Rattus norvegicus
0.0009
-
NADPH
pH 7.0, 25C, mutant Y149F
Rattus norvegicus
9.5
-
NADP+
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
25
-
NADPH
pH 7.0, 25C, wild-type enzyme
Rattus norvegicus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Rattus norvegicus
Other publictions for EC 1.1.1.10
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)
721689
Metz
A novel L-xylulose reductase e ...
Trichoderma reesei, Trichoderma reesei QM9414
Biochemistry
52
2453-2460
2013
-
-
1
-
1
-
-
5
-
-
1
2
-
4
-
-
1
-
-
-
-
-
13
1
-
-
-
5
2
-
-
2
-
-
-
-
-
1
2
-
1
-
-
-
-
5
-
-
1
2
-
-
-
1
-
-
-
-
13
1
-
-
-
5
2
-
-
-
1
4
4
1
-
-
722271
Son
DHS-21, a dicarbonyl/L-xylulos ...
Caenorhabditis elegans
FEBS Lett.
585
1310-1316
2011
-
-
1
-
1
-
-
6
1
-
-
2
-
2
-
-
-
-
-
5
-
-
8
-
-
-
-
6
1
-
-
2
-
-
-
-
-
1
2
-
1
-
-
-
-
6
1
-
-
2
-
-
-
-
-
5
-
-
8
-
-
-
-
6
1
-
-
-
1
3
3
1
6
6
712023
Mojzita
The true L-xylulose reductase ...
Aspergillus niger
FEBS Lett.
584
3540-3544
2010
-
-
1
-
-
-
-
1
-
-
-
-
-
4
-
-
-
-
-
-
3
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
3
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
695778
Matsushika
Efficient bioethanol productio ...
Scheffersomyces stipitis
Appl. Environ. Microbiol.
75
3818-3822
2009
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
695829
Hou
Impact of overexpressing NADH ...
Scheffersomyces stipitis
Appl. Microbiol. Biotechnol.
82
909-919
2009
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
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-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
696889
Krahulec
Engineering of a matched pair ...
Candida tenuis
Biotechnol. J.
4
684-694
2009
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
697218
Zhao
Structure/function analysis of ...
Homo sapiens
Cell. Mol. Life Sci.
66
1570-1579
2009
-
-
1
1
-
-
2
2
-
-
-
-
-
1
-
-
1
-
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-
-
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-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
699148
Branco
-
Profiles of xylose reductase, ...
Meyerozyma guilliermondii, Meyerozyma guilliermondii FTI
J. Chem. Technol. Biotechnol.
84
326-330
2009
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
3
-
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-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
699368
Gurpilhares
The behavior of key enzymes of ...
Meyerozyma guilliermondii
J. Ind. Microbiol. Biotechnol.
36
87-93
2009
-
-
-
-
-
-
1
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
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-
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-
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-
-
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-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
686877
Matsunaga
L-Xylulose reductase is involv ...
Homo sapiens
Free Radic. Biol. Med.
44
1191-1202
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
2
-
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-
-
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-
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-
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-
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-
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-
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-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
687858
Matsushika
Bioethanol production from xyl ...
Scheffersomyces stipitis
J. Biosci. Bioeng.
105
296-299
2008
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
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1
-
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-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
695810
Matsushika
Expression of protein engineer ...
Scheffersomyces stipitis
Appl. Microbiol. Biotechnol.
81
243-255
2008
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
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-
1
-
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1
1
-
-
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-
-
-
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-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684552
Nair
Biochemical characterization o ...
Neurospora crassa
Appl. Environ. Microbiol.
73
2001-2004
2007
-
-
1
-
-
-
-
4
-
-
-
-
-
4
-
-
1
-
-
-
-
-
2
-
1
1
-
2
2
2
-
2
-
-
-
-
-
1
2
-
-
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-
-
-
4
-
-
-
-
-
-
-
1
-
-
-
-
2
-
1
1
-
2
2
2
-
-
-
-
-
-
-
-
688749
Hou
Effect of the reversal of coen ...
Scheffersomyces stipitis
Lett. Appl. Microbiol.
45
184-189
2007
-
-
1
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
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-
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-
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1
-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668392
Matsunaga
Multiplicity of mammalian redu ...
Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Drug Metab. Pharmacokinet.
21
1-18
2006
-
-
-
2
-
-
-
-
-
-
-
4
-
7
-
-
-
-
-
8
-
-
8
4
-
-
3
-
-
-
-
4
-
-
-
-
-
-
4
2
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
8
-
-
8
4
-
-
3
-
-
-
-
-
-
-
-
-
-
-
668491
Sudo
Transgenic mice over-expressin ...
Mus musculus
Exp. Anim.
54
385-394
2005
-
-
1
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670839
El-Kabbani
Structure of the tetrameric fo ...
Homo sapiens, Rattus norvegicus
Proteins
60
424-432
2005
-
-
-
1
4
-
3
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
4
2
-
2
-
-
-
4
1
4
-
2
3
2
-
-
-
-
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656206
Verho
A novel NADH-linked L-xylulose ...
Ambrosiozyma monospora
J. Biol. Chem.
279
14746-14751
2004
-
-
1
-
-
-
-
4
-
1
-
1
-
3
-
-
1
-
-
-
-
-
5
-
1
-
-
-
2
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
4
-
1
-
1
-
-
-
1
-
-
-
-
5
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
656841
Saint-Cyr
P26h and dicarbonyl/L-xylulose ...
Mesocricetus auratus
Mol. Reprod. Dev.
69
137-145
2004
-
-
-
-
-
-
-
-
1
-
1
-
-
4
-
-
-
1
-
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
657322
El-Kabbani
Crystal structure of human L-x ...
Homo sapiens
Proteins
55
724-732
2004
-
-
1
1
2
-
-
6
-
-
-
1
-
3
-
-
-
1
-
-
-
-
3
-
1
-
-
3
1
-
-
2
-
-
-
-
-
1
2
1
2
-
-
-
-
6
-
-
-
1
-
-
-
-
-
-
-
-
3
-
1
-
-
3
1
-
-
-
-
-
-
-
-
-
654438
Ishikura
Structural determinant for col ...
Homo sapiens, Mus musculus
Biochem. Biophys. Res. Commun.
308
68-72
2003
-
-
1
1
6
-
-
-
-
-
-
-
-
7
-
-
1
2
-
-
-
-
4
3
2
-
2
-
2
-
-
4
-
-
-
-
-
1
4
1
6
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
4
3
2
-
2
-
2
-
-
-
-
-
-
-
-
-
654968
Carbone
Structure-based design of inhi ...
Homo sapiens
Bioorg. Med. Chem. Lett.
13
1469-1474
2003
-
1
-
-
-
-
2
-
2
-
-
1
-
2
-
-
-
1
-
1
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
2
-
-
2
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655222
Ishikura
Identification of amino acid r ...
Rattus norvegicus
Chem. Biol. Interact.
143-144
543-550
2003
-
-
1
-
14
-
1
33
1
-
1
2
-
4
-
-
-
1
-
1
-
-
6
1
1
-
-
5
1
-
-
2
-
-
-
-
-
1
2
-
14
-
-
1
-
33
1
-
1
2
-
-
-
-
-
1
-
-
6
1
1
-
-
5
1
-
-
-
-
-
-
-
-
-
656049
Nakagawa
Molecular characterization of ...
Cavia porcellus, Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus
J. Biol. Chem.
277
17888-17891
2002
-
-
1
-
-
-
41
84
1
-
-
-
-
10
-
-
2
5
-
40
2
-
62
-
5
-
-
84
5
-
-
20
-
-
-
-
-
1
20
-
-
-
-
41
-
84
1
-
-
-
-
-
-
2
-
40
2
-
62
-
5
-
-
84
5
-
-
-
-
-
-
-
-
-
287033
Ishikura
Molecular cloning, expression ...
Cricetinae
Chem. Biol. Interact.
130-132
879-889
2001
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
1
1
-
2
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
2
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285666
Metzger
Amino acid substitutions in th ...
Scheffersomyces stipitis
Eur. J. Biochem.
228
50-54
1995
-
-
-
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285665
Witteveen
-
Isolation and characterization ...
Aspergillus niger
Microbiology
140
1679-1685
1994
-
-
-
-
-
-
-
4
-
-
2
1
-
1
-
-
1
-
-
-
2
1
4
1
-
-
-
-
2
2
-
4
-
-
-
-
-
-
4
-
-
-
-
-
-
4
-
-
2
1
-
-
-
1
-
-
2
1
4
1
-
-
-
-
2
2
-
-
-
-
-
-
-
-
246420
Doten
Inducible xylitol dehydrogenas ...
Erwinia sp., Erwinia sp. 4D2P
J. Bacteriol.
162
845-848
1985
-
-
-
-
-
-
-
1
-
-
1
-
-
2
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285658
Doten
Characterization of xylitol-ut ...
Pantoea ananatis
J. Bacteriol.
161
529-533
1985
-
-
1
-
-
-
-
1
-
-
1
-
-
1
-
-
1
-
-
-
1
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
-
1
-
-
-
-
1
-
-
1
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246419
Alizade
Chirality of xylitol-oxidizing ...
Cavia porcellus
FEBS Lett.
67
41-44
1976
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285660
Lowe
Some applications of insolubil ...
Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
48
1004-1010
1972
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246414
Hickman
A sensitive and stereospecific ...
Cavia porcellus
J. Biol. Chem.
234
758-761
1959
-
-
-
-
-
-
3
1
-
-
-
-
-
1
-
-
1
-
-
1
-
1
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
3
-
1
-
-
-
-
-
-
-
1
-
1
-
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
285663
Hollmann
The L-xylulose-xylitol enzyme ...
Cavia porcellus
J. Biol. Chem.
225
87-102
1957
-
-
-
-
-
1
1
-
-
1
-
-
-
1
-
-
-
-
-
1
-
1
2
-
-
-
1
-
1
-
2
2
-
-
-
-
-
-
2
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
1
-
1
2
-
-
-
1
-
1
-
2
-
-
-
-
-
-
-
285664
Touster
The reduction of L-xylulose to ...
Cavia porcellus
J. Biol. Chem.
221
697-709
1954
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