BRENDA - Enzyme Database show
show all sequences of 1.1.1.10

A novel NADH-linked L-xylulose reductase in the L-arabinose catabolic pathway of yeast

Verho, R.; Putkonen, M.; Londesborough, J.; Penttilä, M.; Richard, P.; J. Biol. Chem. 279, 14746-14751 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
construction of a cDNA library, DNA sequence determination and analysis, subcloning in Escherichia coli DH5alpha, overexpression as His-tagged enzyme in Saccharomyces cerevisiae strain CEN.PK2
Ambrosiozyma monospora
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.7
-
D-arabinitol
pH 9.0, 30°C, purified recombinant enzyme
Ambrosiozyma monospora
4.7
-
D-ribulose
pH 7.0, 30°C, purified recombinant enzyme
Ambrosiozyma monospora
7.2
-
L-xylitol
pH 9.0, 30°C, purified recombinant enzyme
Ambrosiozyma monospora
9.6
-
L-xylulose
pH 7.0, 30°C, purified recombinant enzyme
Ambrosiozyma monospora
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Ambrosiozyma monospora
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-xylulose + NADH
Ambrosiozyma monospora
part of the L-arabinose catabolism
L-xylitol + NAD+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Ambrosiozyma monospora
Q70FD1
fragment; yeast, strain NRRL Y-1484
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Saccharomyces cerevisiae by nickel affinity chromatography
Ambrosiozyma monospora
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-ribulose + NADH
-
656206
Ambrosiozyma monospora
D-arabinitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
about 100fold lower activity compared to L-xylulose
656206
Ambrosiozyma monospora
D-arabinitol + NAD+
-
-
-
r
L-xylulose + NADH
-
656206
Ambrosiozyma monospora
L-xylitol + NAD+
-
-
-
r
L-xylulose + NADH
part of the L-arabinose catabolism
656206
Ambrosiozyma monospora
L-xylitol + NAD+
-
-
-
r
additional information
NADH-linked enzyme form, no activity with NADPH and NADP+, no activity with L-arabinitol, adonitol or ribitol, dulcitol or galactitol, D-mannitol, and D-sorbitol, no activity with D-sorbose, L-sorbose, D-psicose, and D-fructose
656206
Ambrosiozyma monospora
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Ambrosiozyma monospora
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
forward, reduction reaction
Ambrosiozyma monospora
9
-
reverse, oxidation reaction
Ambrosiozyma monospora
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
specific for, no activity with NADP+
Ambrosiozyma monospora
NADH
specific for no activity with NADPH
Ambrosiozyma monospora
Cloned(Commentary) (protein specific)
Commentary
Organism
construction of a cDNA library, DNA sequence determination and analysis, subcloning in Escherichia coli DH5alpha, overexpression as His-tagged enzyme in Saccharomyces cerevisiae strain CEN.PK2
Ambrosiozyma monospora
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
specific for, no activity with NADP+
Ambrosiozyma monospora
NADH
specific for no activity with NADPH
Ambrosiozyma monospora
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.7
-
D-arabinitol
pH 9.0, 30°C, purified recombinant enzyme
Ambrosiozyma monospora
4.7
-
D-ribulose
pH 7.0, 30°C, purified recombinant enzyme
Ambrosiozyma monospora
7.2
-
L-xylitol
pH 9.0, 30°C, purified recombinant enzyme
Ambrosiozyma monospora
9.6
-
L-xylulose
pH 7.0, 30°C, purified recombinant enzyme
Ambrosiozyma monospora
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Ambrosiozyma monospora
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-xylulose + NADH
Ambrosiozyma monospora
part of the L-arabinose catabolism
L-xylitol + NAD+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Saccharomyces cerevisiae by nickel affinity chromatography
Ambrosiozyma monospora
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-ribulose + NADH
-
656206
Ambrosiozyma monospora
D-arabinitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
about 100fold lower activity compared to L-xylulose
656206
Ambrosiozyma monospora
D-arabinitol + NAD+
-
-
-
r
L-xylulose + NADH
-
656206
Ambrosiozyma monospora
L-xylitol + NAD+
-
-
-
r
L-xylulose + NADH
part of the L-arabinose catabolism
656206
Ambrosiozyma monospora
L-xylitol + NAD+
-
-
-
r
additional information
NADH-linked enzyme form, no activity with NADPH and NADP+, no activity with L-arabinitol, adonitol or ribitol, dulcitol or galactitol, D-mannitol, and D-sorbitol, no activity with D-sorbose, L-sorbose, D-psicose, and D-fructose
656206
Ambrosiozyma monospora
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Ambrosiozyma monospora
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
forward, reduction reaction
Ambrosiozyma monospora
9
-
reverse, oxidation reaction
Ambrosiozyma monospora
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
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1
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1
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13
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1
4
4
1
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722271
Son
DHS-21, a dicarbonyl/L-xylulos ...
Caenorhabditis elegans
FEBS Lett.
585
1310-1316
2011
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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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1
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6
1
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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
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1
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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
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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
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1
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3
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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
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1
1
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2
2
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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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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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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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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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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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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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668491
Sudo
Transgenic mice over-expressin ...
Mus musculus
Exp. Anim.
54
385-394
2005
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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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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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656841
Saint-Cyr
P26h and dicarbonyl/L-xylulose ...
Mesocricetus auratus
Mol. Reprod. Dev.
69
137-145
2004
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