大麦（Hordeum vulgare）黄化质体膜中原叶绿素酸酯还原酶的底物特异性研究。
Substrate-specificity studies on protochlorophyllide reductase in barley (Hordeum vulgare) etioplast membranes.
作者信息
Griffiths W T
出版信息
Biochem J. 1980 Jan 15;186(1):267-78. doi: 10.1042/bj1860267.
Abstract
- The substrate specificity of the enzyme protochlorophyllide reductase in barley (Hordeum vulgare) etioplasts was investigated. 2. It was shown that naturally occurring esterified protochlorophyllide and chemically prepared protochlorophyllide methyl ester are not substrates for the enzyme, suggesting an important role for the C-7 carboxylic acid group in binding of the porphyrin to the enzyme. 3. Removal of magnesium from the protochlorophyllide leads to inactivity of the compound as a substrate for the enzyme. However, activity can be restored by replacing the magnesium with zinc, whereas nickel, copper or cobalt failed to restore substrate activity. 4. Binding of the second substrate, NADPH, to the enzyme probably occurs through the 2'-phosphate group in the coenzyme.
摘要
- 对大麦（Hordeum vulgare）黄化质体中酶原叶绿素酸酯还原酶的底物特异性进行了研究。2. 结果表明，天然存在的酯化原叶绿素酸酯和化学合成的原叶绿素酸甲酯不是该酶的底物，这表明卟啉的C-7羧酸基团在卟啉与酶的结合中起重要作用。3. 从原叶绿素酸酯中去除镁会导致该化合物作为酶底物失去活性。然而，用锌替代镁可恢复活性，而镍、铜或钴无法恢复底物活性。4. 第二种底物NADPH与酶的结合可能通过辅酶中的2'-磷酸基团发生。
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