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

Scholtz, Rudolf; Messi, Ferruccio; Leisinger, Thomas; Cook, Alasdair M.

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

Dateien

Three_dehalogenases.pdfGröße: 2.04 MBDownloads: 313

Datum

1988

Autor:innen

Scholtz, Rudolf

Messi, Ferruccio

Leisinger, Thomas

Cook, Alasdair M.

URI (zitierfähiger Link)

http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-69998

Link zur Lizenz

Attribution-NonCommercial-NoDerivs 2.0 Generic

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Applied and Environmental Microbiology. 1988, 54(12), pp. 3034-3038

Zusammenfassung

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.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

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. 1988, 54(12), pp. 3034-3038

BibTex

@article{Scholtz1988Three-8332,
  year={1988},
  title={Three dehalogenases and physiological restraints in the biodegradation of haloalkanes by Arthrobacter sp. strain HA1},
  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.}
}

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Universitätsbibliographie

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