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首页> 外文期刊>Journal of Biotechnology >Thermomyces lanuginosus lipase-catalyzed regioselective acylation of nucleosides: Enzyme substrate recognition
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Thermomyces lanuginosus lipase-catalyzed regioselective acylation of nucleosides: Enzyme substrate recognition

机译：嗜热单胞菌脂肪酶催化核苷的区域选择性酰化：酶底物识别

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摘要

Substrate recognition of Thermomyces lanuginosus lipase in the acylation of nucleosides was revealed through rational substrate engineering for the first time. T. lanuginosus lipase displayed higher catalytic activities and excellent 5'-regioselectivities (94->99%) in the acylation of ribonucleosides 1f-1j as compared to those in the acylation of 2'-deoxynucleosides 1a-1e. The higher reaction rates and excellent 5'-regioselectivities might derive from a favorable hydrogen bonding between the 2'-hydroxyl group of 1f-1j and phenolic hydroxyl group of Tyr21 present in the hydrophilic region of the lipase.
机译：首次通过合理的底物工程设​​计揭示了嗜热单胞菌脂酶在核苷酰化中的底物识别。与2'-脱氧核苷1a-1e的酰化反应相比，T。lanuginosus脂肪酶在核糖核苷1f-1j的酰化反应中显示出更高的催化活性和出色的5'-区域选择性（94-> 99％）。较高的反应速率和出色的5'-区域选择性可能源于脂肪酶亲水区域中1f-1j的2'-羟基与Tyr21的酚羟基之间的良好氢键键合。

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