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Literature summary for 1.1.99.36 extracted from

  • Piersma, S.R.; Norin, A.; de Vries, S.; Jornvall, H.; Duine, J.A.
    Inhibition of nicotinoprotein (NAD+-containing) alcohol dehydrogenase by trans-4-(N,N-dimethylamino)-cinnamaldehyde binding to the active site (2003), J. Protein Chem., 22, 457-461.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
docking study of trans-4-(N,N-dimethylamino)-cinnamaldehyde to the enzyme model active site. The np-ADH model accommodates the inhibitor in a substrate-like conformation without collision with inner-sphere and secondary sphere residues Amycolatopsis methanolica

Inhibitors

Inhibitors Comment Organism Structure
trans-4-(N,N-dimethylamino)-cinnamaldehyde inhibition through direct binding to the catalytic zinc ion in a substrate-like geometry. This binding is accompanied by a characteristic red shift of the aldehyde absorbance from 398 nm to 467 nm Amycolatopsis methanolica

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ takes part in catalysis Amycolatopsis methanolica

Organism

Organism UniProt Comment Textmining
Amycolatopsis methanolica P80175
-
-

Synonyms

Synonyms Comment Organism
np-ADH
-
Amycolatopsis methanolica

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0016
-
trans-4-(N,N-dimethylamino)-cinnamaldehyde uncompetitive inhibition term reflecting binding to the enzyme containing the oxidized coenzyme Amycolatopsis methanolica
0.0033
-
trans-4-(N,N-dimethylamino)-cinnamaldehyde competitive inhibition term with respect to NDMA Amycolatopsis methanolica