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Biocatalysis with Unnatural Amino Acids: Enzymology Meets Xenobiology
Author(s) -
Agostini Federica,
Völler JanStefan,
Koksch Beate,
AcevedoRocha Carlos G.,
Kubyshkin Vladimir,
Budisa Nediljko
Publication year - 2017
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.201610129
Subject(s) - biocatalysis , protein engineering , chemistry , synthetic biology , biochemical engineering , amino acid , mutagenesis , biochemistry , enzyme , computational biology , biology , catalysis , engineering , mutation , reaction mechanism , gene
The goal of xenobiology is to design biological systems endowed with unusual biochemical functions, whereas enzymology concerns the study of enzymes, the workhorses of biocatalysis. Biocatalysis employs enzymes and organisms to perform useful biotransformations in synthetic chemistry and biotechnology. During the past few years, the effects of incorporating noncanonical amino acids (ncAAs) into enzymes with potential applications in biocatalysis have been increasingly investigated. In this Review, we provide an overview of the effects of new chemical functionalities that have been introduced into proteins to improve various facets of enzymatic catalysis. We also discuss future research avenues that will complement unnatural mutagenesis with standard protein engineering to produce novel and versatile biocatalysts with applications in synthetic organic chemistry and biotechnology.