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Literature summary for 1.2.1.3 extracted from

  • Eggert, M.W.; Byrne, M.E.; Chambers, R.P.
    Kinetic involvement of acetaldehyde substrate inhibition on the rate equation of yeast aldehyde dehydrogenase (2012), Appl. Biochem. Biotechnol., 168, 824-833.
    View publication on PubMed
Search for more literature for 1.2.1.3

Inhibitors

Inhibitors Comment Organism Structure
acetaldehyde acetaldehyde inhibition of the enzyme is initiated below concentrations of 0.05 mM in the presence of 0.5 mM NAD or less Saccharomyces cerevisiae
NADH while acetaldehyde alone (1.6 mM) as an inhibiting factor yields a relative rate around 38% of the maximum experimental rate, the result with 0.18 mM initial NADH is 13% of the maximum experimental rate and further declines to 6.5% at 0.4 mM NADH Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + NAD+ + H2O
-
 Saccharomyces cerevisiae acetate + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
ALDH
-
 Saccharomyces cerevisiae
NAD-aldehyde dehydrogenase
-
 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.162
-
 NADH at 22°C and pH 7.8 Saccharomyces cerevisiae
2.55
-
 acetaldehyde at 22°C and pH 7.8 Saccharomyces cerevisiae