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Three dehalogenases and physiological restraints in the biodegradation of haloalkanes by Arthrobacter sp. strain HA1

Three dehalogenases and physiological restraints in the biodegradation of haloalkanes by Arthrobacter sp. strain HA1

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SCHOLTZ, Rudolf, Ferruccio MESSI, Thomas LEISINGER, Alasdair M. COOK, 1988. Three dehalogenases and physiological restraints in the biodegradation of haloalkanes by Arthrobacter sp. strain HA1. In: Applied and Environmental Microbiology. 54(12), pp. 3034-3038

@article{Scholtz1988Three-8332, title={Three dehalogenases and physiological restraints in the biodegradation of haloalkanes by Arthrobacter sp. strain HA1}, year={1988}, number={12}, volume={54}, journal={Applied and Environmental Microbiology}, pages={3034--3038}, author={Scholtz, Rudolf and Messi, Ferruccio and Leisinger, Thomas and Cook, Alasdair M.} }

2011-03-24T17:42:44Z Cook, Alasdair M. Three dehalogenases and physiological restraints in the biodegradation of haloalkanes by Arthrobacter sp. strain HA1 Scholtz, Rudolf application/pdf deposit-license Arthrobacter sp. strain HA1 utilizes 18 C2-to-C8 1-haloalkanes for growth and synthesizes an inducible 1-bromoalkane debrominase of unknown physiological function (R. Scholtz, T. Leisinger, F. Suter, and A.M. Cook, J. Bacteriol. 169:5016-5021, 1987) in addition to an inducible 1-chlorohexane halidohydrolase which dehalogenates some 50 substrates, including alpha, omega-dihaloalkanes. alpha, omega-Dihaloalkanes were utilized by cultures of strain HA1 under certain conditions only. C9 and C8 homologs prevented growth. At suitable concentrations, C7-to-C5 homologs could serve as sole sources of carbon and energy for growth. C4 and C3 homologs could be utilized only in the presence of a second substrate (e.g., butanol), and the C2 homolog was not degraded. Kinetics of growth and substrate utilization indicated that cells of strain HA1 growing in butanol-salts medium could be used to test whether compounds induced the 1-chlorohexane halidohydrolase. No gratuitous induction of synthesis of the enzyme was observed. Many enzyme substrates (e.g., bromobenzene) did not induce synthesis of the enzyme, though the enzyme sequence to degrade the product (phenol) was present. Some inducers (e.g., bromomethane) were enzyme substrates but not growth substrates. In an attempt to find a physiological role for the 1-bromoalkane debrominase, we observed that several long-chain haloaliphatic compounds (>C9; e.g., 1-bromohexadecane and 1-chlorohexadecane) were utilized for growth and that induced cells could dehalogenate several 1-haloalkanes (at least C4 to C16). The dehalogenation of the long-chain compounds could not be assayed in the cell extract, so we presume that a third haloalkane dehalogenase was present. All dehalogenations were equally active in the presence or absence of molecular oxygen and were presumed to be hydrolytic. Leisinger, Thomas eng First publ. in: Applied and Environmental Microbiology 54 (1988), 12, pp. 3034-3038 Scholtz, Rudolf 1988 Messi, Ferruccio 2011-03-24T17:42:44Z Messi, Ferruccio Leisinger, Thomas Cook, Alasdair M.

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