BRENDA - Enzyme Database show
show all sequences of 1.1.1.113

Comparative study on the mutated xylose reductase to increase ethanol production in xylose-utilizing Saccharomyces cerevisiae strains

Xiong, M.; Woodruff, A.; Tang, X.; Tian, X.; Zhang, J.; Cao, L.; J. Taiwan Inst. Chem. Eng. 44, 605-610 (2013)
No PubMed abstract available

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
K270D/N272P/S271G/R276F
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
K270G
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
K270M
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
K270R
mutant shows a 3.4fold and 2.4fold higher NADPH and NADH preferred xylose reductase activities, respectively, compared with wild-type. Mutant exhibits an improved xylose consumption rate, balanced redox system and increased ethanol yield and production rate
Saccharomyces cerevisiae
K270R/N272D
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
K270R/R276H
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
K274R
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
K274R/N276D
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
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Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K270D/N272P/S271G/R276F
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
K270G
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
K270M
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
K270R
mutant shows a 3.4fold and 2.4fold higher NADPH and NADH preferred xylose reductase activities, respectively, compared with wild-type. Mutant exhibits an improved xylose consumption rate, balanced redox system and increased ethanol yield and production rate
Saccharomyces cerevisiae
K270R/N272D
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
K270R/R276H
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
K274R
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
K274R/N276D
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
Saccharomyces cerevisiae
Other publictions for EC 1.1.1.113
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)
738984
Zhang
Rapid ethanol production at el ...
Neurospora crassa
Metab. Eng.
31
140-152
2015
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725843
Xiong
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Comparative study on the mutat ...
Saccharomyces cerevisiae
J. Taiwan Inst. Chem. Eng.
44
605-610
2013
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8
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639098
Bonete
Glucose dehydrogenase from the ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
FEBS Lett.
383
227-229
1996
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285763
Uehara
L-Xylose dehydrogenase in bake ...
Saccharomyces cerevisiae
J. Biochem.
52
461-463
1962
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