甲壳动物血蓝蛋白向儿茶酚氧化酶的转化。
Conversion of crustacean hemocyanin to catecholoxidase.
作者信息
Jaenicke Elmar, Decker Heinz
机构信息
Institut für Molekulare Biophysik, Johannes Gutenberg-Universität, 55099 Mainz, Germany.
出版信息
Micron. 2004;35(1-2):89-90. doi: 10.1016/j.micron.2003.10.027.
PMID:15036301
Abstract
Crustacean hemocyanin as oxygen carrier and catecholoxidase as enzymes belong to the same protein family (type 3 copper proteins) sharing very similar active sites. Treatment with SDS of these hemocyanins results in an opening of the entrance to the active site for bulky phenolic compounds. This demonstrates, that almost all hemocyanin subunits possess the ability of catecholoxidase activity.
摘要
作为氧载体的甲壳动物血蓝蛋白和作为酶的儿茶酚氧化酶属于同一蛋白质家族（3型铜蛋白），具有非常相似的活性位点。用十二烷基硫酸钠处理这些血蓝蛋白会导致活性位点入口对大分子酚类化合物开放。这表明，几乎所有血蓝蛋白亚基都具有儿茶酚氧化酶活性。
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