Abstract
The potential of biocatalysis becomes increasingly recognized as an efficient and green tool for modern organic synthesis. Biocatalytic promiscuity, a new frontier extended the use of enzymes in organic synthesis, has attracted much attention and expanded rapidly in the past decade. It focuses on the enzyme catalytic activities with unnatural substrates and alternative chemical transformations. Exploiting enzyme catalytic unconventional reactions might lead to improvements in existing catalysts and provide novel synthesis pathways that are currently not available. Among these enzymes, hydrolase (such as lipase, protease, acylase) undoubtedly has received special attention since they display remarkable activities for some unexpected reactions such as aldol reaction and other novel carbon-carbon and carbon-heteroatom bond-forming reactions. This chapter introduces the recent progress in hydrolase catalytic unconventional reactions and application in organic synthesis. Some important examples of hydrolase catalytic unconventional reactions in addition reactions are reviewed, highlighting the catalytic promiscuity of hydrolases focuses on aldol reaction, Michael addition, and multicomponent reactions.
Highlights
Biocatalysis is the application of enzymes for chemical transformations of organic compounds
In order to preliminarily explore the mechanism of the reaction, site-directed mutagenesis was performed on the hydrolysis catalytic triad of BioH, and the results indicated “alternate-site enzyme promiscuity.”
This chapter has reviewed some examples of various types of hydrolase catalytic promiscuous reactions and their applications in the past decade
Summary
Biocatalysis is the application of enzymes for chemical transformations of organic compounds. Enzymes act in a temperature range of 20–40°C, under neutral aqueous, and in the absence of substrate functional group protection This minimizes problems of undesired side reactions such as decomposition, isomerization, racemization, and rearrangement, which often plague traditional methodology; (4) enzymes display high chemoselectivity, regioselectivity, and enantioselectivity. There is an enzyme-catalyzed process equivalent to almost every type of organic reaction, such as oxidation, hydrolysis, addition, halogenation, alkylation, and isomerization. The main work in our group will be disclosed, highlighting the catalytic properties of hydrolases to catalyze single processes and multicomponent and tandem reactions. The promiscuous hydrolase-catalyzed reactions are outlined with focus on Michael addition, aldol reaction, Mannich reaction, Biginelli reaction, etc
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