College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, Shanghai 201620, China.
Appl Biochem Biotechnol. 2010 Nov;162(5):1506-16. doi: 10.1007/s12010-009-8856-9. Epub 2010 Apr 11.
Some features of native enzyme's active site were used to conjunction with a chemical reagent or modifying group, which would generate new functionality different from the natural enzyme. In order to obtain an efficient catalyst, we have designed four different molecular size N-derivatives of modifiers and introduced them into the active site of papain to obtain new semisynthetic enzymes, which were used as catalyst in reduction of benzaldehyde to yield benzyl alcohol respectively, and the reactions carried out with recycling agent in 0.1 M phosphate buffer pH 6.5 at 37 degrees C. The results had shown that a longer N-derivative of semisynthetic enzyme had higher catalytic activity. Furthermore, we propose a plausible model for the catalytic mechanism in the semisynthetic enzymes system.
利用天然酶活性部位的某些特征与化学试剂或修饰基团结合,会产生不同于天然酶的新功能。为了获得高效的催化剂,我们设计了四种不同分子大小的 N-衍生物修饰剂,并将其引入木瓜蛋白酶的活性部位,得到了新的半合成酶,分别将它们用作还原苯甲醛生成苯甲醇的催化剂,并在 37°C、0.1 M 磷酸盐缓冲液 pH 6.5 中使用回收试剂进行反应。结果表明,半合成酶的 N-衍生物较长时具有更高的催化活性。此外,我们还对半合成酶体系的催化机制提出了一个合理的模型。