BRENDA - Enzyme Database show
show all sequences of 1.1.1.10

Structural determinant for cold inactivation of rodent L-xylulose reductase

Ishikura, S.; Usami, N.; El-Kabbani, O.; Hara, A.; Biochem. Biophys. Res. Commun. 308, 68-72 (2003)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Mus musculus
Crystallization (Commentary)
Crystallization
Organism
crystal structure analysis and modelling
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
D238E
site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation
Mus musculus
D238E/L242W
site-directed mutagenesis, mutation leads to complete prevention of cold inactivation, mutant exists in tetrameric form at low temperature
Mus musculus
D238E/L242W/T244C
site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
Mus musculus
L242W
site-directed mutagenesis, mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
Mus musculus
L242W/T244C
site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
Mus musculus
T244C
site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation
Mus musculus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type and mutant enzymes from Escherichia coli
Mus musculus
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
Mus musculus
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
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacetyl + NAD(P)H
dicarbonyl reductase activity
654438
Mus musculus
acetoin + NAD(P)+
-
-
-
r
diacetyl + NAD(P)H
dicarbonyl reductase activity
654438
Homo sapiens
acetoin + NAD(P)+
-
-
-
r
L-xylulose + NADPH + H+
-
654438
Mus musculus
L-xylitol + NADP+
-
-
-
r
L-xylulose + NADPH + H+
-
654438
Homo sapiens
L-xylitol + NADP+
-
-
-
r
Subunits
Subunits
Commentary
Organism
More
the dimeric form is inactive
Mus musculus
tetramer
amino acid residues Trp242, Glu238, Arg203, and Cys244 are important for tetramer formation
Homo sapiens
tetramer
amino acid residues Trp242, Glu238, Arg203, and Cys244 are important for tetramer formation
Mus musculus
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Homo sapiens
25
-
assay at
Mus musculus
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
additional information
-
stable at low temperatures
Homo sapiens
additional information
-
dissociation into inactive dimers at low temperatures
Mus musculus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Homo sapiens
7
-
assay at
Mus musculus
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Mus musculus
NADP+
-
Homo sapiens
NADPH
-
Mus musculus
NADPH
-
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Mus musculus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Mus musculus
NADP+
-
Homo sapiens
NADPH
-
Mus musculus
NADPH
-
Homo sapiens
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure analysis and modelling
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D238E
site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation
Mus musculus
D238E/L242W
site-directed mutagenesis, mutation leads to complete prevention of cold inactivation, mutant exists in tetrameric form at low temperature
Mus musculus
D238E/L242W/T244C
site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
Mus musculus
L242W
site-directed mutagenesis, mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
Mus musculus
L242W/T244C
site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
Mus musculus
T244C
site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation
Mus musculus
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant enzymes from Escherichia coli
Mus musculus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacetyl + NAD(P)H
dicarbonyl reductase activity
654438
Mus musculus
acetoin + NAD(P)+
-
-
-
r
diacetyl + NAD(P)H
dicarbonyl reductase activity
654438
Homo sapiens
acetoin + NAD(P)+
-
-
-
r
L-xylulose + NADPH + H+
-
654438
Mus musculus
L-xylitol + NADP+
-
-
-
r
L-xylulose + NADPH + H+
-
654438
Homo sapiens
L-xylitol + NADP+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
More
the dimeric form is inactive
Mus musculus
tetramer
amino acid residues Trp242, Glu238, Arg203, and Cys244 are important for tetramer formation
Homo sapiens
tetramer
amino acid residues Trp242, Glu238, Arg203, and Cys244 are important for tetramer formation
Mus musculus
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Homo sapiens
25
-
assay at
Mus musculus
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
additional information
-
stable at low temperatures
Homo sapiens
additional information
-
dissociation into inactive dimers at low temperatures
Mus musculus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Homo sapiens
7
-
assay at
Mus musculus
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
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1
2
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4
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1
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13
1
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5
2
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2
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1
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1
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1
2
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1
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13
1
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5
2
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-
1
4
4
1
-
-
722271
Son
DHS-21, a dicarbonyl/L-xylulos ...
Caenorhabditis elegans
FEBS Lett.
585
1310-1316
2011
-
-
1
-
1
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6
1
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2
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2
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5
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8
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6
1
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1
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1
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6
1
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2
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5
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8
-
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6
1
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-
1
3
3
1
6
6
712023
Mojzita
The true L-xylulose reductase ...
Aspergillus niger
FEBS Lett.
584
3540-3544
2010
-
-
1
-
-
-
-
1
-
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4
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3
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1
1
1
1
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695778
Matsushika
Efficient bioethanol productio ...
Scheffersomyces stipitis
Appl. Environ. Microbiol.
75
3818-3822
2009
-
-
1
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2
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1
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695829
Hou
Impact of overexpressing NADH ...
Scheffersomyces stipitis
Appl. Microbiol. Biotechnol.
82
909-919
2009
-
-
1
-
-
-
-
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3
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1
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696889
Krahulec
Engineering of a matched pair ...
Candida tenuis
Biotechnol. J.
4
684-694
2009
-
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1
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4
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1
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697218
Zhao
Structure/function analysis of ...
Homo sapiens
Cell. Mol. Life Sci.
66
1570-1579
2009
-
-
1
1
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-
2
2
-
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1
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1
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1
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1
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1
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1
1
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699148
Branco
-
Profiles of xylose reductase, ...
Meyerozyma guilliermondii, Meyerozyma guilliermondii FTI
J. Chem. Technol. Biotechnol.
84
326-330
2009
-
-
-
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2
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3
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699368
Gurpilhares
The behavior of key enzymes of ...
Meyerozyma guilliermondii
J. Ind. Microbiol. Biotechnol.
36
87-93
2009
-
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1
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3
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1
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686877
Matsunaga
L-Xylulose reductase is involv ...
Homo sapiens
Free Radic. Biol. Med.
44
1191-1202
2008
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4
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687858
Matsushika
Bioethanol production from xyl ...
Scheffersomyces stipitis
J. Biosci. Bioeng.
105
296-299
2008
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1
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695810
Matsushika
Expression of protein engineer ...
Scheffersomyces stipitis
Appl. Microbiol. Biotechnol.
81
243-255
2008
-
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1
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3
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684552
Nair
Biochemical characterization o ...
Neurospora crassa
Appl. Environ. Microbiol.
73
2001-2004
2007
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1
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4
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4
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1
1
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2
2
2
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688749
Hou
Effect of the reversal of coen ...
Scheffersomyces stipitis
Lett. Appl. Microbiol.
45
184-189
2007
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1
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2
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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
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2
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4
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7
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668491
Sudo
Transgenic mice over-expressin ...
Mus musculus
Exp. Anim.
54
385-394
2005
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1
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670839
El-Kabbani
Structure of the tetrameric fo ...
Homo sapiens, Rattus norvegicus
Proteins
60
424-432
2005
-
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1
4
-
3
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5
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2
1
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4
2
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4
1
4
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2
3
2
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2
1
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656206
Verho
A novel NADH-linked L-xylulose ...
Ambrosiozyma monospora
J. Biol. Chem.
279
14746-14751
2004
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1
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4
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1
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1
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3
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656841
Saint-Cyr
P26h and dicarbonyl/L-xylulose ...
Mesocricetus auratus
Mol. Reprod. Dev.
69
137-145
2004
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1
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1
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4
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1
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