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Monobody-mediated alteration of enzyme specificity.


ABSTRACT: Current methods for engineering enzymes modify enzymes themselves and require a detailed mechanistic understanding or a high-throughput assay. Here, we describe a new approach where catalytic properties are modulated with synthetic binding proteins, termed monobodies, directed to an unmodified enzyme. Using the example of a ?-galactosidase from Bacillus circulans, we efficiently identified monobodies that restricted its substrates for its transgalactosylation reaction and selectively enhanced the production of small oligosaccharide prebiotics.

SUBMITTER: Tanaka S 

PROVIDER: S-EPMC4989918 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature

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Monobody-mediated alteration of enzyme specificity.

Tanaka Shun-Ichi S   Takahashi Tetsuya T   Koide Akiko A   Ishihara Satoru S   Koikeda Satoshi S   Koide Shohei S  

Nature chemical biology 20150831 10


Current methods for engineering enzymes modify enzymes themselves and require a detailed mechanistic understanding or a high-throughput assay. Here, we describe a new approach where catalytic properties are modulated with synthetic binding proteins, termed monobodies, directed to an unmodified enzyme. Using the example of a β-galactosidase from Bacillus circulans, we efficiently identified monobodies that restricted its substrates for its transgalactosylation reaction and selectively enhanced th  ...[more]

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