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Literature summary for 1.1.1.1 extracted from

  • Abuin, E.; Lissi, E.; Leon, L.
    Kinetics of ethanol oxidation catalyzed by yeast alcohol dehydrogenase in aqueous solutions of sodium dodecylsulfate (2008), Protein J., 27, 247-252.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
SDS in the presence of the surfactant the initial reaction rates are consistently lower than in pure buffer at all the surfactant concentrations considered (0.5-50 mM). This effect is mainly due to an increase in the dissociation constant of beta-NAD+ which reaches its maximum value (7.1 mM) at the critical micelle concentration. Above the critical micelle concentration the effect of the surfactant is mainly due to an increase in the Michaels constants of the alcohol, with values of 41 mM for 15 mM SDS and 50 mM for 50 mM SDS Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.24
-
beta-NAD+ in presence of 0.5 mM SDS Saccharomyces cerevisiae
0.243
-
beta-NAD+ in presence of 0.5 mM SDS Saccharomyces cerevisiae
0.35
-
beta-NAD+ in presence of 1 mM SDS Saccharomyces cerevisiae
0.71
-
beta-NAD+ in presence of 3 mM SDS Saccharomyces cerevisiae
1.23
-
beta-NAD+ in presence of 50 mM SDS Saccharomyces cerevisiae
2.29
-
beta-NAD+ in presence of 15 mM SDS Saccharomyces cerevisiae
13
-
ethanol in presence of 0.5 mM SDS Saccharomyces cerevisiae
14
-
ethanol in presence of 3 mM SDS Saccharomyces cerevisiae
17
-
ethanol in presence of 1 mM SDS Saccharomyces cerevisiae
41
-
ethanol in presence of 15 mM SDS Saccharomyces cerevisiae
50
-
ethanol in presence of 50 mM SDS Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ethanol + beta-NAD+
-
Saccharomyces cerevisiae acetaldehyde + NADH + H+
-
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