The haloacid operon of Burkholderia sp. MBA4 is catabolically repressed

Session: Biofilms - Keynotepublished_or_final_versio

Draft Genome Sequence of the Haloacid-Degrading Burkholderia caribensis Strain MBA4

Burkholderia caribensis MBA4 was isolated from soil for its ability to utilize 2-haloacid. An inducible haloacid operon, encoding for a dehalogenase and a permease, is mainly responsible for the biotransformation. Here, we report the draft genome sequence of this strain.postprin

Complete Genome Sequence of the Exopolysaccharide-Producing Burkholderia caribensis Type Strain MWAP64

We report the complete genome sequence of Burkholderia caribensis MWAP64 (LMG 18531), which was isolated from soil for its proficiency in producing large amounts of exopolysaccharide that help form microaggregates in a vertisol. There are four replicons with a total size of 9,032,119 bp.published_or_final_versio

Biochemical and structural studies of a L-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii

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

Expression of water hyacinth metallothionein gene in yeast

06-Biotechnology and industrial applications: Abstracts Poster Sessio

Molecular biology of the burkholderia cepacia complex

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De novo assembly of the genome of a haloacid degrading Burkholderia caribensis

Escherichia coli and coagulase-positive Staphylococcus are recognised as major zoonotic pathogens causing serious infection in both humans and animals. Recently, there has been an increase in the prevalence of multidrug-resistant E. coli and methicillin-resistant Staphylococcus spp. in both humans and animals around the globe. The Australian Group on Antimicrobial Resistance perform period-prevalence studies to monitor changes in antimicrobial resistance in these pathogens when they cause clinical infections in hum…link_to_OA_fulltex