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Biochemical and structural studies of a L-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii
Authors
A Diez
AA Vagin
+29 more
Andrey A. Lebedev
CA Rye
Carrie A. Rye
Number 4 CCP4. Collaborative Computational Project
CN Pace
G Vriend
GN Murshudov
IS Ridder
IS Ridder
J Ploeg van der
JD Allpress
Jennifer A. Littlechild
JH Slater
JH Slater
JQ Liu
JSH Tsang
K Motosugi
Michail N. Isupov
P Emsley
P Mallick
P Potterton
R Arai
RA Laskowski
RM Esnouf
T Hisano
T Kurihara
Y Kawarabayasi
YF Li
Z Otwinowski
Publication date
18 November 2013
Publisher
'Springer Science and Business Media LLC'
Doi
Cite
Abstract
addresses: Henry Wellcome Building for Biocatalysis, School of Biosciences, University of Exeter, Stocker Road, Exeter EX4 4QD, UK.types: Journal Article; Research Support, Non-U.S. Gov'tThis a post-print, author-produced version of an article accepted for publication in Extremophiles. Copyright © 2009 Springer Verlag. The definitive version is available at http://link.springer.com/article/10.1007%2Fs00792-008-0208-0Haloacid dehalogenases have potential applications in the pharmaceutical and fine chemical industry as well as in the remediation of contaminated land. The L: -2-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii has been cloned and over-expressed in Escherichia coli and successfully purified to homogeneity. Here we report the structure of the recombinant dehalogenase solved by molecular replacement in two different crystal forms. The enzyme is a homodimer with each monomer being composed of a core-domain of a beta-sheet bundle surrounded by alpha-helices and an alpha-helical sub-domain. This fold is similar to previously solved mesophilic L: -haloacid dehalogenase structures. The monoclinic crystal form contains a putative inhibitor L: -lactate in the active site. The enzyme displays haloacid dehalogenase activity towards carboxylic acids with the halide attached at the C2 position with the highest activity towards chloropropionic acid. The enzyme is thermostable with maximum activity at 60 degrees C and a half-life of over 1 h at 70 degrees C. The enzyme is relatively stable to solvents with 25% activity lost when incubated for 1 h in 20% v/v DMSO
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Last time updated on 04/12/2019
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Open Research Exeter
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oai:ore.exeter.ac.uk:10871/139...
Last time updated on 15/12/2013