Silent catalytic promiscuity in the high-fidelity terpene cyclase δ-cadinene synthase
نویسندگان
چکیده
منابع مشابه
The amino-terminal segment in the β-domain of δ-cadinene synthase is essential for catalysis.
Despite its distance from the active site the flexible amino-terminal segment (NTS) in the β-domain of the plant sesquiterpene cyclase δ-cadinene synthase (DCS) is essential for active site closure and desolvation events during catalysis.
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δ-Cadinene synthase is a sesquiterpene cyclase that utilises the universal achiral precursor farnesyl diphosphate (FDP) to generate predominantly the bicyclic sesquiterpene δ-cadinene and about 2 % germacradien-4-ol, which is also generated from FDP by the cyclase germacradien-4-ol synthase. Herein, the mechanism by which sesquiterpene synthases discriminate between deprotonation and reaction w...
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Enzyme promiscuity is a concept that in the last years is earning prominence in different fields of enzymology like biocatalysis, enzyme engineering or enzyme evolution. Catalytic promiscuity is defined as the ability of an enzyme to catalyze more than one chemical transformation. Naturally occurring catalytic promiscuity provide the starting point for a Darwinian evolution of enzymes to new fu...
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In recent years, it has become increasingly clear that promiscuity plays a key role in the evolution of new enzyme function. This finding has helped to elucidate fundamental aspects of molecular evolution. While there has been extensive experimental work on enzyme promiscuity, computational modeling of the chemical details of such promiscuity has traditionally fallen behind the advances in expe...
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ژورنال
عنوان ژورنال: Organic & Biomolecular Chemistry
سال: 2019
ISSN: 1477-0520,1477-0539
DOI: 10.1039/c8ob02821d