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Literature summary for 1.1.1.4 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
Search for more literature for 1.1.1.4

Protein Variants

Protein Variants Comment Organism
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
E221S/I222R mutant with preference for NADPH as coenzyme Saccharomyces cerevisiae
E221S/I222R/A223S mutant with preference for NADPH as coenzyme Saccharomyces cerevisiae

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P39714
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Saccharomyces cerevisiae