Unknown

Dataset Information

0

Rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes.


ABSTRACT: Enzymes that catalyze carbon-carbon bond formation can be exploited as biocatalyst for synthetic organic chemistry. However, natural enzymes frequently do not possess the required properties or specificities to catalyze industrially useful transformations. This mini-review describes recent work using knowledge-guided site-specific mutagenesis of key active site residues to alter substrate specificity, stereospecificity and reaction specificity of these enzymes. In addition, examples of de novo designed enzymes that catalyze C-C bond reactions not found in nature will be discussed.

SUBMITTER: Baker P 

PROVIDER: S-EPMC3962088 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

altmetric image

Publications

Rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes.

Baker Perrin P   Seah Stephen Y K SY  

Computational and structural biotechnology journal 20121002


Enzymes that catalyze carbon-carbon bond formation can be exploited as biocatalyst for synthetic organic chemistry. However, natural enzymes frequently do not possess the required properties or specificities to catalyze industrially useful transformations. This mini-review describes recent work using knowledge-guided site-specific mutagenesis of key active site residues to alter substrate specificity, stereospecificity and reaction specificity of these enzymes. In addition, examples of de novo d  ...[more]

Similar Datasets

| S-EPMC3962203 | biostudies-literature
| S-EPMC5113669 | biostudies-literature
| S-EPMC6698183 | biostudies-literature
| S-EPMC6915740 | biostudies-literature
| S-EPMC3432936 | biostudies-literature
| S-EPMC6051890 | biostudies-literature
| S-EPMC6458069 | biostudies-literature
| S-EPMC3547142 | biostudies-literature
| S-EPMC3136257 | biostudies-literature
| S-EPMC4222288 | biostudies-literature