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Literature summary extracted from

  • Ehsani, M.; Fernandez, M.R.; Biosca, J.A.; Dequin, S.
    Reversal of coenzyme specificity of 2,3-butanediol dehydrogenase from Saccharomyces cerevisae and in vivo functional analysis (2009), Biotechnol. Bioeng., 104, 381-389.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.4 E221S the mutation produces a 170fold decrease in the Vm/Km with NADH because of a simultaneous 16fold increase in the Km value and an 11fold decrease in the Vm value, the mutation provides a positive effect on NADPH coenzyme specificity Saccharomyces cerevisiae
1.1.1.4 E221S/I222R mutant with preference for NADPH as coenzyme Saccharomyces cerevisiae
1.1.1.4 E221S/I222R/A223S mutant with preference for NADPH as coenzyme Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.4 0.044
-
 NADPH mutant enzyme E221S/I222R Saccharomyces cerevisiae
1.1.1.4 0.044
-
 NADPH mutant enzyme E221S/I222R/A223S Saccharomyces cerevisiae
1.1.1.4 0.045
-
 NADH wild type enzyme Saccharomyces cerevisiae
1.1.1.4 0.087
-
 NADPH mutant enzyme E221S Saccharomyces cerevisiae
1.1.1.4 0.7
-
 NADH mutant enzyme E221S Saccharomyces cerevisiae
1.1.1.4 3
-
 (R)-acetoin wild type enzyme Saccharomyces cerevisiae
1.1.1.4 33
-
 (R)-acetoin mutant enzyme E221S/I222R/A223S Saccharomyces cerevisiae
1.1.1.4 77
-
 (R)-acetoin mutant enzyme E221S/I222R Saccharomyces cerevisiae
1.1.1.4 161
-
 (R)-acetoin mutant enzyme E221S Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.4 Saccharomyces cerevisiae P39714
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.4 0.1
-
 wild type enzyme, using 1 mM NADPH as cosubstrate Saccharomyces cerevisiae
1.1.1.4 4.1
-
 mutant enzyme E221S, using 1 mM NADH as cosubstrate Saccharomyces cerevisiae
1.1.1.4 4.8
-
 mutant enzyme E221S/I222R, using 1 mM NADH as cosubstrate Saccharomyces cerevisiae
1.1.1.4 6.1
-
 mutant enzyme E221S/I222R/A223S, using 1 mM NADH as cosubstrate Saccharomyces cerevisiae
1.1.1.4 13.7
-
 mutant enzyme E221S, using 1 mM NADPH as cosubstrate Saccharomyces cerevisiae
1.1.1.4 54.7
-
 mutant enzyme E221S/I222R, using 1 mM NADPH as cosubstrate Saccharomyces cerevisiae
1.1.1.4 92
-
 wild type enzyme, using 1 mM NADH as cosubstrate Saccharomyces cerevisiae
1.1.1.4 93.2
-
 mutant enzyme E221S/I222R/A223S, using 1 mM NADPH as cosubstrate Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.4 (R)-acetoin + NADH + H+
-
 Saccharomyces cerevisiae (2R,3R)-butane-2,3-diol + NAD+
-
 ?
1.1.1.4 (R)-acetoin + NADPH + H+ wild type enzyme does not use NADPH as coenzyme Saccharomyces cerevisiae (2R,3R)-butane-2,3-diol + NADP+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.4 (2R,3R)-2,3-butanediol dehydrogenase
-
 Saccharomyces cerevisiae
1.1.1.4 BDH1
-
 Saccharomyces cerevisiae
1.1.1.4 NAD(H)-dependent 2,3-butanediol dehydrogenase
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.4 NADH
-
 Saccharomyces cerevisiae