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show all sequences of 1.1.1.117

Role of Saccharomyces cerevisiae oxidoreductases Bdh1p and Ara1p in the metabolism of acetoin and 2,3-butanediol

Gonzalez, E.; Fernandez, M.R.; Marco, D.; Calam, E.; Sumoy, L.; Pares, X.; Dequin, S.; Biosca, J.A.; Appl. Environ. Microbiol. 76, 670-679 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli as a His-tagged fusion protein
Saccharomyces cerevisiae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Purification (Commentary)
Commentary
Organism
partial; using Ni-NTA chromatography
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R/S)-acetoin + NADPH
Ara1p is as an oxidoreductase that can reduce racemic acetoin to meso-2,3-butanediol and (2S,3S)-2,3-butanediol in the presence of NADPH
710944
Saccharomyces cerevisiae
(2S,3S)-2,3-butanediol + NADP+
-
-
-
?
additional information
enzyme in addition acts as a NADPH-dependent oxidoreductase producing meso-2,3-butanediol and (2S,3S)-2,3-butanediol from (R,S)-acetoin
710944
Saccharomyces cerevisiae
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli as a His-tagged fusion protein
Saccharomyces cerevisiae
Purification (Commentary) (protein specific)
Commentary
Organism
partial; using Ni-NTA chromatography
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R/S)-acetoin + NADPH
Ara1p is as an oxidoreductase that can reduce racemic acetoin to meso-2,3-butanediol and (2S,3S)-2,3-butanediol in the presence of NADPH
710944
Saccharomyces cerevisiae
(2S,3S)-2,3-butanediol + NADP+
-
-
-
?
additional information
enzyme in addition acts as a NADPH-dependent oxidoreductase producing meso-2,3-butanediol and (2S,3S)-2,3-butanediol from (R,S)-acetoin
710944
Saccharomyces cerevisiae
?
-
-
-
-
General Information
General Information
Commentary
Organism
malfunction
a double mutant DELATbdh1 and DELTA ara1 strain still produces (2S,3S)-2,3-butanediol and meso-2,3-butanediol suggesting only a minor role of Ara1p in the production of 2,3-butanediol
Saccharomyces cerevisiae
General Information (protein specific)
General Information
Commentary
Organism
malfunction
a double mutant DELATbdh1 and DELTA ara1 strain still produces (2S,3S)-2,3-butanediol and meso-2,3-butanediol suggesting only a minor role of Ara1p in the production of 2,3-butanediol
Saccharomyces cerevisiae
Other publictions for EC 1.1.1.117
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)
710944
Gonzalez
Role of Saccharomyces cerevisi ...
Saccharomyces cerevisiae
Appl. Environ. Microbiol.
76
670-679
2010
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285774
Kim
D-Arabinose dehydrogenase and ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1429
29-39
1998
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4
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10663
Kim
D-Arabinose dehydrogenase and ...
Candida albicans
Biochim. Biophys. Acta
1297
1-8
1996
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6
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389443
Metzger
Partial purification of rat li ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
26
742-747
1967
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285790
Cline
The isolation of three sugar d ...
Pseudomonas sp., Pseudomonas sp. G6
J. Biol. Chem.
240
4488-4492
1965
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285791
Cline
Enzymatic characterization and ...
Pseudomonas sp., Pseudomonas sp. G6
J. Biol. Chem.
240
4493-4497
1965
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285797
Cline
Some physical properties of th ...
Pseudomonas sp., Pseudomonas sp. G6
J. Biol. Chem.
240
4498-4502
1965
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