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Apoenzyme Reconstitution as a Chemical Tool for Structural Enzymology and Biotechnology
Author(s) -
Fruk Ljiljana,
Kuo ChiHsien,
Torres Eduardo,
Niemeyer Christof M.
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200803098
Subject(s) - cofactor , biocatalysis , enzyme , chemistry , function (biology) , yield (engineering) , biochemistry , biology , catalysis , materials science , reaction mechanism , evolutionary biology , metallurgy
Enzymes with artificial cofactors : Nondiffusible organic cofactors of enzymes can often be replaced by artifical analogues to generate semisynthetic enzymes (see scheme). This approach can be used to study structure–function relationships in enzymology and to produce novel enzymes with enhanced or even entirely new functions that are useful for biosensing, biocatalysis, and materials science applications.Many enzymes contain a nondiffusible organic cofactor, often termed a prosthetic group, which is located in the active site and essential for the catalytic activity of the enzyme. These cofactors can often be extracted from the protein to yield the respective apoenzyme, which can subsequently be reconstituted with an artificial analogue of the native cofactor. Nowadays a large variety of synthetic cofactors can be used for the reconstitution of apoenzymes and, thus, generate novel semisynthetic enzymes. This approach has been refined over the past decades to become a versatile tool of structural enzymology to elucidate structure–function relationships of enzymes. Moreover, the reconstitution of apoenzymes can also be used to generate enzymes possessing enhanced or even entirely new functionality. This Review gives an overview on historical developments and the current state‐of‐the‐art on apoenzyme reconstitution.