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ACS Chem Biol. 2018 Jun 15;13(6):1487-1492. doi: 10.1021/acschembio.8b00384. Epub 2018 May 18.

Monobody-Mediated Alteration of Lipase Substrate Specificity.

Author information

1
Department of Biochemistry and Molecular Biology , The University of Chicago , Chicago , Illinois 60637 , United States.
2
Frontier Research Department, Gifu R&D Center , Amano Enzyme, Inc. , Gifu 509-0109 , Japan.
3
Ritsumeikan Global Innovation Research Organization , Ritsumeikan University , 1-1-1 Noji-higashi , Shiga 525-8577 , Japan.
4
Department of Biotechnology, College of Life Sciences , Ritsumeikan University , 1-1-1 Noji-higashi , Shiga 525-8577 , Japan.
5
Perlmutter Cancer Center , New York University Langone Medical Center , New York , New York 10016 , United States.
6
Department of Medicine , New York University School of Medicine , New York , New York 10016 , United States.
7
Department of Biochemistry and Molecular Pharmacology , New York University School of Medicine , New York , New York 10016 , United States.

Abstract

Controlling the catalytic properties of enzymes remain an important challenge in chemistry and biotechnology. We have recently established a strategy for altering enzyme specificity in which the addition of proxy monobodies, synthetic binding proteins, modulates the specificity of an otherwise unmodified enzyme. Here, in order to examine its broader applicability, we employed the strategy on Candida rugosa lipase 1 (CRL1), an enzyme with a tunnel-like substrate binding site. We successfully identified proxy monobodies that restricted the substrate specificity of CRL1 toward short-chain fatty acids. The successes with this enzyme system and a β-galactosidase used in the previous work suggest that our strategy can be applied to diverse enzymes with distinct architectures of substrate binding sites.

PMID:
29757606
DOI:
10.1021/acschembio.8b00384

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