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Literature summary extracted from

  • Heidlas, J.; Tressl, R.
    Purification and characterization of a (R)-2,3-butanediol dehydrogenase from Saccharomyces cerevisiae (1990), Arch. Microbiol., 154, 267-273.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.303 Mg2+ activation, (R)-2,3-butanediol dehydrogenase activity Saccharomyces cerevisiae
1.1.1.303 Mn2+ activation, (R)-2,3-butanediol dehydrogenase activity Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.4
-
 Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.4 dipicolinate
-
 Saccharomyces cerevisiae
1.1.1.4 EDTA
-
 Saccharomyces cerevisiae
1.1.1.4 o-phenanthroline
-
 Saccharomyces cerevisiae
1.1.1.303 dipicolinate inhibition, (R)-2,3-butanediol dehydrogenase activity Saccharomyces cerevisiae
1.1.1.303 EDTA inhibition, (R)-2,3-butanediol dehydrogenase activity Saccharomyces cerevisiae
1.1.1.303 o-phenanthroline inhibition, (R)-2,3-butanediol dehydrogenase activity Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.4 Mg2+ activation Saccharomyces cerevisiae
1.1.1.4 Mn2+ activation Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.4 35000
-
 4 * 35000, SDS-PAGE Saccharomyces cerevisiae
1.1.1.4 140000
-
 gel filtration Saccharomyces cerevisiae
1.1.1.303 35000
-
 4 * 35000, SDS-PAGE Saccharomyces cerevisiae
1.1.1.303 140000
-
 gel filtration Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.4 Saccharomyces cerevisiae
-
-
-
1.1.1.303 Saccharomyces cerevisiae
-
 bifunctional diacetyl reductase and (R)-2,3-butanediol dehydrogenase
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.303
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.4 (R,S)-3-hydroxy-2-pentanone + NADH
-
 Saccharomyces cerevisiae 2,3-pentanediol + NAD+
-
 r
1.1.1.4 (R,S)-4-hydroxy-3-pentanone + NADH
-
 Saccharomyces cerevisiae 2,3-pentanediol + NAD+
-
 r
1.1.1.4 1,2-butanediol + NAD+
-
 Saccharomyces cerevisiae ?
-
 ?
1.1.1.4 1,2-propanediol + NAD+
-
 Saccharomyces cerevisiae ?
-
 ?
1.1.1.4 1-hydroxy-2-butanone + NADH
-
 Saccharomyces cerevisiae ?
-
 ?
1.1.1.4 2,3-butanediol + NAD+ 2,3-butanediol without specification of stereochemistry Saccharomyces cerevisiae acetoin + NADH
-
 r
1.1.1.4 2,3-butanediol + NAD+ oxidation occurs selectively at the (R)-center of 2,3-butanediol Saccharomyces cerevisiae acetoin + NADH
-
 r
1.1.1.4 2,3-pentanediol + NAD+ racemate Saccharomyces cerevisiae 4-hydroxy-3-pentanone + 3-hydroxy-2-pentanone + NADH
-
 r
1.1.1.4 acetoin + NADH + H+
-
 Saccharomyces cerevisiae 2,3-butanediol + NAD+
-
 r
1.1.1.4 diacetyl + NADH
-
 Saccharomyces cerevisiae 2,3-butanediol + NAD+
-
 ?
1.1.1.4 hydroxyacetone + NADH
-
 Saccharomyces cerevisiae 1,2-propanediol
-
 ?
1.1.1.303 1,2-cyclohexanedione + NADH + H+ 5% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin Saccharomyces cerevisiae (R)-2-hydroxy-1-cyclohexanone + NAD+
-
 ir
1.1.1.303 2,3-pentanedione + NADH + H+ 7% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin Saccharomyces cerevisiae (3R)-3-hydroxy-2-pentanone + NAD+
-
 ir
1.1.1.303 diacetyl + NADH + H+ 21% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin Saccharomyces cerevisiae (R)-acetoin + NAD+
-
 ir
1.1.1.303 additional information enzyme is specific for NADH Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.4 tetramer 4 * 35000, SDS-PAGE Saccharomyces cerevisiae
1.1.1.303 tetramer 4 * 35000, SDS-PAGE Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
1.1.1.4 (R)-2,3-butanediol dehydrogenase
-
 Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.4 6.7
-
 substrate reduction Saccharomyces cerevisiae
1.1.1.4 7.2
-
 substrate oxidation Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.303 NADH enzyme is specific for NADH Saccharomyces cerevisiae