Site-directed mutagenesis of dienelactone hydrolase produces dienelactone isomerase

Ian Walker; Christopher J. Easton; David L. Ollis

doi:10.1039/b000365o

Site-directed mutagenesis of dienelactone hydrolase produces dienelactone isomerase

Ian Walker
, Christopher J. Easton^*
, David L. Ollis

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

Abstract

Replacing the active site Cys-123 of dienelactone hydrolase with Ser completely changes the catalysis displayed by the protein, from hydrolysis of the substrate E- and Z-dienelactones to maleylacetate by the native enzyme, to interconversion of the substrates by the mutant, dienelactone isomerase.

Original language	English
Pages (from-to)	671-672
Number of pages	2
Journal	Chemical Communications
Issue number	8
DOIs	https://doi.org/10.1039/b000365o
Publication status	Published - 21 Apr 2000

Access to Document

10.1039/b000365o

Cite this

@article{6d328e0bdf4140f6bf17e1c2dd0041b3,

title = "Site-directed mutagenesis of dienelactone hydrolase produces dienelactone isomerase",

abstract = "Replacing the active site Cys-123 of dienelactone hydrolase with Ser completely changes the catalysis displayed by the protein, from hydrolysis of the substrate E- and Z-dienelactones to maleylacetate by the native enzyme, to interconversion of the substrates by the mutant, dienelactone isomerase.",

author = "Ian Walker and Easton, \{Christopher J.\} and Ollis, \{David L.\}",

year = "2000",

month = apr,

day = "21",

doi = "10.1039/b000365o",

language = "English",

pages = "671--672",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "8",

}

TY - JOUR

T1 - Site-directed mutagenesis of dienelactone hydrolase produces dienelactone isomerase

AU - Walker, Ian

AU - Easton, Christopher J.

AU - Ollis, David L.

PY - 2000/4/21

Y1 - 2000/4/21

N2 - Replacing the active site Cys-123 of dienelactone hydrolase with Ser completely changes the catalysis displayed by the protein, from hydrolysis of the substrate E- and Z-dienelactones to maleylacetate by the native enzyme, to interconversion of the substrates by the mutant, dienelactone isomerase.

AB - Replacing the active site Cys-123 of dienelactone hydrolase with Ser completely changes the catalysis displayed by the protein, from hydrolysis of the substrate E- and Z-dienelactones to maleylacetate by the native enzyme, to interconversion of the substrates by the mutant, dienelactone isomerase.

UR - https://www.scopus.com/pages/publications/0034696912

U2 - 10.1039/b000365o

DO - 10.1039/b000365o

M3 - Article

SN - 1359-7345

SP - 671

EP - 672

JO - Chemical Communications

JF - Chemical Communications

IS - 8

ER -

Site-directed mutagenesis of dienelactone hydrolase produces dienelactone isomerase

Abstract

Access to Document

Other files and links

Fingerprint

Cite this