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Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase

Date

Authors

Kim, Hye-Kyung

Liu, Jian-Wei

Carr, Paul D

Ollis, David

Publisher

Munksgaard International Publishers

Abstract

The enzyme dienelactone hydrolase (DLH) has undergone directed evolution to produce a series of mutant proteins that have enhanced activity towards the non-physiological substrates α-naphthyl acetate and p-nitrophenyl acetate. In terms of steady-state ki

Keywords

Keywords: 1 naphthyl acetate; alpha-naphthyl acetate; benzylsulfonyl fluoride; carboxylesterase; carboxymethylenebutenolidase; naphthol derivative; article; binding site; chemistry; directed molecular evolution; drug antagonism; enzyme specificity; enzymology; Esch

URI

http://hdl.handle.net/1885/81927

Collections

ANU Research Publications

Source

Acta Crystallographica Section D: Biological Crystallography

Type

Journal article

DOI

10.1107/S0907444905009042

Restricted until

2037-12-31

Downloads

File

Description

01_Kim_Following_directed_evolution_2005.pdf (964.41 KB)