polycyclic compound
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2016 ◽  
Vol 122 ◽  
pp. 247-256 ◽  
Author(s):  
Benedetta Maggio ◽  
Maria Valeria Raimondi ◽  
Demetrio Raffa ◽  
Fabiana Plescia ◽  
Marie-Christine Scherrmann ◽  
...  

Nanoscale ◽  
2014 ◽  
Vol 6 (2) ◽  
pp. 678-682 ◽  
Author(s):  
Su-Young Son ◽  
Yong-Jin Noh ◽  
Changsuk Bok ◽  
Sungho Lee ◽  
Byoung Gak Kim ◽  
...  

2010 ◽  
Vol 28 (8) ◽  
pp. 1379-1384
Author(s):  
Xiuhui Lu ◽  
Yuehua Xu ◽  
Zhenxia Lian ◽  
Yongqing Li

1997 ◽  
Vol 62 (14) ◽  
pp. 4857-4861 ◽  
Author(s):  
Cheng-Tung Lin ◽  
Nae-Jen Wang ◽  
Hsien-Zong Tseng ◽  
Teh-Chang Chou

1987 ◽  
Vol 52 (8) ◽  
pp. 2107-2113 ◽  
Author(s):  
Marie Stiborová ◽  
Sylva Leblová

Rape alcohol dehydrogenase (ADH) is inhibited by heterocyclic compounds with a five- to six-membered ring (imidazole, pyrazole, 4-methylpyrazole, 3-methylpyrazole, pyridine, nicotine amide) and by o-phenanthroline, a heterocyclic, polycyclic compound. Pyrazole and its derivatives, imidazole and pyridine, are competitive inhibitors with respect to ethanol. Nicotine amide and o-phenanthroline behave as mixed inhibitors (competitive – noncompetitive) with respect to the substrate. The addition of Zn2+-ions to the reaction medium interferes with the competition by o-phenanthroline. 4-Methylpyrazole and pyrazole are the strongest inhibitors of rape ADH. 2-Mercaptoethanol is an inhibitor of rape ADH which competes with ethanol and the coenzyme. The reversible inhibition by mercaptoethanol changes into the irreversible inactivation of the enzyme. The binding of inhibitors to the zinc atom present in the molecule of rape ADH and the localization of the metal in the enzyme protein have been studied.


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