Circular permutation: a different way to engineer enzyme structure and function.

Abstract:

:Protein engineers traditionally rely on amino acid substitutions to alter the functional properties of biomacromolecules, yet have largely overlooked the potential benefits of reorganizing the polypeptide chain of a protein by circular permutation (CP). By connecting the native protein termini via a covalent linker and introducing new ends through the cleavage of an existing peptide bond, CP can perturb local tertiary structure and protein dynamics, as well as introduce possible quaternary structure changes. In several recent studies, these effects have successfully been exploited to manipulate protein scaffolds, resulting in improved catalytic activity and altered substrate or ligand binding affinity, as well as enabling the design of novel biocatalysts and biosensors.

journal_name

Trends Biotechnol

journal_title

Trends in biotechnology

authors

Yu Y,Lutz S

doi

10.1016/j.tibtech.2010.10.004

subject

Has Abstract

pub_date

2011-01-01 00:00:00

pages

18-25

issue

1

eissn

0167-7799

issn

1879-3096

pii

S0167-7799(10)00178-2

journal_volume

29

pub_type

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