Three dehalogenases and physiological restraints in the biodegradation of haloalkanes by Arthrobacter sp. strain HA1
Abstract
Arthrobacter sp. strain HA1 utilizes 18 C{sub 2}-to-C{sub 8} 1-haloalkanes for growth and synthesizes an inducible 1-bromoalkane debrominase of unknown physiological function in addition to an inducible 1-chlorohexane halidohydrolase which dehalogenates some 50 substrates, including {alpha},{omega}-dihaloalkanes were utilized by cultures of strain HA1 under certain conditions only. 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 (>C{sub 9}; e.g., 1-bromohexadecane and 1-chlorohexadecane) were utilized for growth and that induced cells could dehalogenate several 1-haloalkanes (at least C{sub 4} to C{sub 16}). 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 andmore »
- Authors:
-
- Swiss Federal Institute of Technology, Zurich (Switzerland)
- Publication Date:
- OSTI Identifier:
- 5131719
- Resource Type:
- Journal Article
- Journal Name:
- Water Resources Research; (USA)
- Additional Journal Information:
- Journal Volume: 54:12; Journal ID: ISSN 0043-1397
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; BACTERIA; METABOLISM; HALOGENATED ALIPHATIC HYDROCARBONS; BIODEGRADATION; HYDROLASES; ENZYME ACTIVITY; AFFINITY; BROMINE COMPOUNDS; ENZYME INDUCTION; PHENOL; SUBSTRATES; TOXICITY; AROMATICS; CHEMICAL REACTIONS; DECOMPOSITION; ENZYMES; GENE REGULATION; HALOGEN COMPOUNDS; HYDROXY COMPOUNDS; MICROORGANISMS; ORGANIC COMPOUNDS; ORGANIC HALOGEN COMPOUNDS; PHENOLS; 550500* - Metabolism
Citation Formats
Scholtz, R, Messi, F, Leisinger, T, and Cook, A M. Three dehalogenases and physiological restraints in the biodegradation of haloalkanes by Arthrobacter sp. strain HA1. United States: N. p., 1988.
Web.
Scholtz, R, Messi, F, Leisinger, T, & Cook, A M. Three dehalogenases and physiological restraints in the biodegradation of haloalkanes by Arthrobacter sp. strain HA1. United States.
Scholtz, R, Messi, F, Leisinger, T, and Cook, A M. 1988.
"Three dehalogenases and physiological restraints in the biodegradation of haloalkanes by Arthrobacter sp. strain HA1". United States.
@article{osti_5131719,
title = {Three dehalogenases and physiological restraints in the biodegradation of haloalkanes by Arthrobacter sp. strain HA1},
author = {Scholtz, R and Messi, F and Leisinger, T and Cook, A M},
abstractNote = {Arthrobacter sp. strain HA1 utilizes 18 C{sub 2}-to-C{sub 8} 1-haloalkanes for growth and synthesizes an inducible 1-bromoalkane debrominase of unknown physiological function in addition to an inducible 1-chlorohexane halidohydrolase which dehalogenates some 50 substrates, including {alpha},{omega}-dihaloalkanes were utilized by cultures of strain HA1 under certain conditions only. 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 (>C{sub 9}; e.g., 1-bromohexadecane and 1-chlorohexadecane) were utilized for growth and that induced cells could dehalogenate several 1-haloalkanes (at least C{sub 4} to C{sub 16}). 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.},
doi = {},
url = {https://www.osti.gov/biblio/5131719},
journal = {Water Resources Research; (USA)},
issn = {0043-1397},
number = ,
volume = 54:12,
place = {United States},
year = {Thu Dec 01 00:00:00 EST 1988},
month = {Thu Dec 01 00:00:00 EST 1988}
}