Substrate specificity of lipase from Burkholderia cepacia in the synthesis of 3'-arylaliphatic acid esters of floxuridine.
Substrate specificity of lipase from Burkholderia cepacia in the synthesis of 3'-arylaliphatic acid esters of floxuridine.
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DOI：
10.1016/j.jbiotec.2009.06.005
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发表时间：
2009-07
影响因子：
4.1
通讯作者：
Ning Li;Q. Zeng;Min-hua Zong
中科院分区：
文献类型：
--
作者：
Ning Li;Q. Zeng;Min-hua Zong
在5种酰基中含有苯环的乙烯基酯中，洋葱伯克霍尔德菌脂肪酶对4-苯基丁酸乙烯酯的专一性最强。随着酰基链长度的增加，酶的3′-区域选择性增强。利用酶促法合成了亲脂性的3′-芳基脂肪酸酯，具有较高的转化率（>98%）和良好的区域选择性（85-99%）。
Among the five vinyl esters bearing phenyl ring in acyl moiety, the lipase from Burkholderia cepacia was most specific toward vinyl 4-phenylbutyrate. Additionally, 3′-regioselectivity of the enzyme was enhanced with the increment of acyl chain length. The lipophilic 3′-arylaliphatic acid esters of floxuridine, its potential prodrugs, were synthesized with high conversions (>98%) and good to excellent regioselectivities (85–99%) via the enzymatic approach.