BRENDA - Enzyme Database
show all sequences of 1.1.1.303

Purification and characterization of a (R)-2,3-butanediol dehydrogenase from Saccharomyces cerevisiae

Heidlas, J.; Tressl, R.; Arch. Microbiol. 154, 267-273 (1990)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Mg2+
activation, (R)-2,3-butanediol dehydrogenase activity
Saccharomyces cerevisiae
Mn2+
activation, (R)-2,3-butanediol dehydrogenase activity
Saccharomyces cerevisiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
dipicolinate
inhibition, (R)-2,3-butanediol dehydrogenase activity
Saccharomyces cerevisiae
EDTA
inhibition, (R)-2,3-butanediol dehydrogenase activity
Saccharomyces cerevisiae
o-phenanthroline
inhibition, (R)-2,3-butanediol dehydrogenase activity
Saccharomyces cerevisiae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
4 * 35000, SDS-PAGE
Saccharomyces cerevisiae
140000
-
gel filtration
Saccharomyces cerevisiae
Organism
Organism
UniProt
Commentary
Textmining
Saccharomyces cerevisiae
-
bifunctional diacetyl reductase and (R)-2,3-butanediol dehydrogenase
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
1,2-cyclohexanedione + NADH + H+
5% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
246410
Saccharomyces cerevisiae
(R)-2-hydroxy-1-cyclohexanone + NAD+
-
-
-
ir
2,3-pentanedione + NADH + H+
7% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
246410
Saccharomyces cerevisiae
(3R)-3-hydroxy-2-pentanone + NAD+
-
-
-
ir
diacetyl + NADH + H+
21% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
246410
Saccharomyces cerevisiae
(R)-acetoin + NAD+
-
-
-
ir
additional information
enzyme is specific for NADH
246410
Saccharomyces cerevisiae
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
tetramer
4 * 35000, SDS-PAGE
Saccharomyces cerevisiae
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
enzyme is specific for NADH
Saccharomyces cerevisiae
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Mg2+
activation, (R)-2,3-butanediol dehydrogenase activity
Saccharomyces cerevisiae
Mn2+
activation, (R)-2,3-butanediol dehydrogenase activity
Saccharomyces cerevisiae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
enzyme is specific for NADH
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
dipicolinate
inhibition, (R)-2,3-butanediol dehydrogenase activity
Saccharomyces cerevisiae
EDTA
inhibition, (R)-2,3-butanediol dehydrogenase activity
Saccharomyces cerevisiae
o-phenanthroline
inhibition, (R)-2,3-butanediol dehydrogenase activity
Saccharomyces cerevisiae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
4 * 35000, SDS-PAGE
Saccharomyces cerevisiae
140000
-
gel filtration
Saccharomyces cerevisiae
Purification (Commentary) (protein specific)
Commentary
Organism
-
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
1,2-cyclohexanedione + NADH + H+
5% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
246410
Saccharomyces cerevisiae
(R)-2-hydroxy-1-cyclohexanone + NAD+
-
-
-
ir
2,3-pentanedione + NADH + H+
7% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
246410
Saccharomyces cerevisiae
(3R)-3-hydroxy-2-pentanone + NAD+
-
-
-
ir
diacetyl + NADH + H+
21% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
246410
Saccharomyces cerevisiae
(R)-acetoin + NAD+
-
-
-
ir
additional information
enzyme is specific for NADH
246410
Saccharomyces cerevisiae
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 35000, SDS-PAGE
Saccharomyces cerevisiae
Other publictions for EC 1.1.1.303
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
Synonyms
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)
246413
Gonzalez
Characterization of a (2R,3R)- ...
Saccharomyces cerevisiae
J. Biol. Chem.
275
35876-35885
2000
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246410
Heidlas
Purification and characterizat ...
Saccharomyces cerevisiae
Arch. Microbiol.
154
267-273
1990
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