Directed evolution combined with rational design increases activity of GpdQ toward a non-physiological substrate and alters the oligomeric structure of the enzyme

Date

2011

Authors

Yip, Sylvia
Foo, Jee
Schenk, Gerhard
Gahan, Lawrence
Carr, Paul D
Ollis, David

Journal Title

Journal ISSN

Volume Title

Publisher

Oxford University Press

Abstract

Directed evolution was used to enhance the activity of the glycerophosphodiesterase enzyme from Enterobacter aerogenes, GpdQ, toward bis(para-nitrophenol) phosphate (BpNPP), a substrate that is frequently used to assay phosphodiesterases. Native GpdQ has

Description

Keywords

Keywords: Accessible surface areas; Active site; Cysteine residues; Dimeric molecules; Directed evolution; Disulfide bonds; Elevated temperature; Enterobacter aerogenes; glycerophosphodiesterase; Hexamers; Low level; Mutant proteins; Native enzymes; Oligomeric stat directed evolution; glycerophosphodiesterase; oligomeric state; rational design

Citation

Source

Protein Engineering Design and Selection

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

10.1093/protein/gzr048

Restricted until

2037-12-31