| Autor: |
Piersma SR; Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden., Norin A, de Vries S, Jörnvall H, Duine JA |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of protein chemistry [J Protein Chem] 2003 Jul; Vol. 22 (5), pp. 457-61. |
| DOI: |
10.1023/b:jopc.0000005461.53788.ee |
| Abstrakt: |
Ethanol oxidation by nicotinoprotein alcohol dehydrogenase (np-ADH) from the bacterium Amycolatopsis methanolica is inhibited by trans-4-(N,N-dimethylamino)-cinnamaldehyde 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. Np-ADH is structurally related to mammalian ADH class I, and a model of np-ADH shows how the cinnamaldehyde derivative can be accommodated in the active site of the nicotinoprotein, correlating the structural and enzymological data. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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