Biocatalytic domino reaction: synthesis of 2H-1-benzopyran-2-one derivatives using alkaline protease from Bacillus licheniformis

Wang, Chang‐Heng; Guan, Zhi; He, Yan‐Hong

doi:10.1039/c0gc00799d

Cited by 50 publications

(21 citation statements)

References 35 publications

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“…This reaction is named after Emil Knoevenagel who first reported this reaction in 1898. [81] Two enzymes, porcine pancreatic lipase [82] and Bacillus licheniformis alkaline protease, [83] have been shown to catalyze Knoevenagel condensation. The reaction catalyzed by porcine lipase was demonstrated with a series of benzaldehyde derivatives ( 85 ) and methylcyanoacetate ( 86 ) in ethanol (Figure 22b).…”

Section: Condensation Reactionsmentioning

confidence: 99%

The Enzymology of Organic Transformations: A Survey of Name Reactions in Biological Systems

2017

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Chemical reactions that are named in honor of their true or at least perceived discoverers are known as “name reactions”. This review is a collection of biological representatives of named chemical reactions. Emphasis is placed on reaction types and catalytic mechanisms that showcase both the chemical diversity in natural product biosynthesis as well as the parallels with synthetic organic chemistry. An attempt has been made to describe the enzymatic mechanisms of catalysis within the context of their synthetic counterparts whenever possible and to discuss the mechanistic hypotheses for those reactions that are presently active areas of investigation. This review has been categorized by reaction type, e.g., condensation, nucleophilic addition, reduction and oxidation, substitution, carboxylation, radical-mediated, and rearrangements, which are subdivided by named reactions.

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Section: Condensation Reactionsmentioning

confidence: 99%

The Enzymology of Organic Transformations: A Survey of Name Reactions in Biological Systems

2017

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“…A series of tandem processes have been reported involving an initial Knoevenagel reaction, leading to the preparation of interesting organic compounds. 2 H ‐1‐Benzopyran‐2‐ones have been obtained through a domino Knoevenagel reaction–intramolecular transesterification catalyzed by BLAP in organic solvent . A significant influence in the chemoselectivity of the reaction has been observed in terms of solvent, water content and temperature, parameters that affect the ratio of the desired benzopyran‐2‐one derivative and the byproduct obtained by domino Knoevenagel–intramolecular hemiketalization (Scheme ).…”

Section: Carbon–carbon Bond‐formation Reactionsmentioning

confidence: 99%

Recent Advances in Biocatalytic Promiscuity: Hydrolase‐Catalyzed Reactions for Nonconventional Transformations

López-Iglesias

Gotor‐Fernández

2015

The Chemical Record

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Enzymes has emerged in recent decades as ideal catalysts for synthetic transformations in mild reaction conditions. Their capacity to accelerate a myriad of biotransformations with high levels of selectivity and broad substrate specificity including excellent atom economy has led to a current full recognition. The six classes of enzymes (oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases) possess outstanding abilities to perform specific modifications in target molecules. Nevertheless, in the last fifteen years, novel examples have appeared related to nonconventional processes catalyzed by various classes of biocatalysts. Amongst these, hydrolases have received special attention since they display remarkable activities in initially unexpected reactions such as carbon-carbon and carbon-heteroatom bond formation reactions, oxidative processes and novel hydrolytic transformations. In this review, the main findings in this area will be disclosed, highlighting the catalytic properties of hydrolases not only to catalyze single processes but also multicomponent and tandem nonconventional reactions.

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“…The derivatives of 2H-1-benzopyran-2-one form the scaffold of many pharmaceuticals [56,57]. Wang et al [58] have used an alkaline protease from B. licheniformis to obtain these by domino Knoevanagel/intramolecular transesterification reactions in low water containing organic solvents.…”

Section: Catalytic Promiscuity: Beyond Lipasesmentioning

confidence: 99%

Enzyme promiscuity: using the dark side of enzyme specificity in white biotechnology

Arora

Mukherjee

Gupta

2014

Sustain Chem Process

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Enzyme promiscuity can be classified into substrate promiscuity, condition promiscuity and catalytic promiscuity. Enzyme promiscuity results in far larger ranges of organic compounds which can be obtained by biocatalysis. While early examples mostly involved use of lipases, more recent literature shows that catalytic promiscuity occurs more widely and many other classes of enzymes can be used to obtain diverse kinds of molecules. This is of immense relevance in the context of white biotechnology as enzyme catalysed reactions use greener conditions.

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Biocatalytic domino reaction: synthesis of 2H-1-benzopyran-2-one derivatives using alkaline protease from Bacillus licheniformis

Cited by 50 publications

References 35 publications

The Enzymology of Organic Transformations: A Survey of Name Reactions in Biological Systems

The Enzymology of Organic Transformations: A Survey of Name Reactions in Biological Systems

Recent Advances in Biocatalytic Promiscuity: Hydrolase‐Catalyzed Reactions for Nonconventional Transformations

Enzyme promiscuity: using the dark side of enzyme specificity in white biotechnology

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