Biochemical and molecular characterisation of the 2,3-dichloro-1-propanol dehalogenase and stereospecific haloalkanoic dehalogenases from a versatile Agrobacterium sp

We previously reported the presence of both haloalcohol and haloalkanoate dehalogenase activity in the Agrobacterium sp. strain NHG3. The versatile nature of the organism led us to further characterise the genetic basis of these dehalogenation activities. Cloning and sequencing of the haloalcohol de...

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Published inBiodegradation (Dordrecht) Vol. 16; no. 5; pp. 485 - 492
Main Authors HIGGINS, Timothy P, HOPE, Stephen J, EFFENDI, Agus J, DAWSON, Shula, DANCER, Brian N
Format Journal Article
LanguageEnglish
Published Dordrecht Springer 01.10.2005
Springer Nature B.V
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Summary:We previously reported the presence of both haloalcohol and haloalkanoate dehalogenase activity in the Agrobacterium sp. strain NHG3. The versatile nature of the organism led us to further characterise the genetic basis of these dehalogenation activities. Cloning and sequencing of the haloalcohol dehalogenase and subsequent analysis suggested that it was part of a highly conserved catabolic gene cluster. Characterisation of the haloalkanoate dehalogenase enzyme revealed the presence of two stereospecific enzymes with a narrow substrate range which acted on D-2-chloropropionic and L-2-chloropropionoic acid, respectively. Cloning and sequencing indicated that the two genes were separated by 87 bp of non-coding DNA and were preceded by a putative transporter gene 66 bp upstream of the D-specific enzyme.
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ISSN:0923-9820
1572-9729
DOI:10.1007/s10532-004-5670-5