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 | 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 | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | takes part in catalysis | Amycolatopsis methanolica |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Amycolatopsis methanolica | P80175 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
np-ADH | - |
Amycolatopsis methanolica |
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 |