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Thermomyces lanuginosus lipase-catalyzed regioselective acylation of nucleosides: Enzyme substrate recognition

Paper ID Volume ID Publish Year Pages File Format Full-Text
24253 43507 2009 4 PDF Available
Title
Thermomyces lanuginosus lipase-catalyzed regioselective acylation of nucleosides: Enzyme substrate recognition
Abstract

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.

Keywords
Thermomyces lanuginosus lipase; Nucleoside; Substrate recognition; Substrate engineering; Enzymatic acylation; Regioselectivity
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Thermomyces lanuginosus lipase-catalyzed regioselective acylation of nucleosides: Enzyme substrate recognition
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 140, Issues 3–4, 25 March 2009, Pages 250–253
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Don't Miss Today's Special Offer
Price was $35.95
You save - $31
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