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| rdf:type
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| Description
| - Haloalkane dehalogenases are bacterial enzymes capable of carbon-halogen bond cleavage in halogenated compounds. To obtain insight in the mechanism of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB), we studied the steady-state and pre-steady-state kinetics of the conversion of the substrates 1-chlorohexane, chlorocyclohexane and bromocyclohexane. The results lead to a proposal of a minimal kinetic mechanism consisting of three main steps: (i) substrate binding, (ii) cleavage of the carbon-halogen bond with simultaneous formation of an alkyl-enzyme intermediate and (iii) hydrolysis of the alkyl-enzyme intermediate. Release of both products, halide and alcohol, is a fast process that was not included in reaction mechanism as a distinct step. Comparison of the kinetic mechanism of LinB with that of haloalkane dehalogenase DhlA from Xantobacter autotrophicus GJ10 and the haloalkane dehalogenase DhaA from Rhodococcus rhodochrous NCIMB 13064 shows that the overall mechanisms are simi
- Haloalkane dehalogenases are bacterial enzymes capable of carbon-halogen bond cleavage in halogenated compounds. To obtain insight in the mechanism of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB), we studied the steady-state and pre-steady-state kinetics of the conversion of the substrates 1-chlorohexane, chlorocyclohexane and bromocyclohexane. The results lead to a proposal of a minimal kinetic mechanism consisting of three main steps: (i) substrate binding, (ii) cleavage of the carbon-halogen bond with simultaneous formation of an alkyl-enzyme intermediate and (iii) hydrolysis of the alkyl-enzyme intermediate. Release of both products, halide and alcohol, is a fast process that was not included in reaction mechanism as a distinct step. Comparison of the kinetic mechanism of LinB with that of haloalkane dehalogenase DhlA from Xantobacter autotrophicus GJ10 and the haloalkane dehalogenase DhaA from Rhodococcus rhodochrous NCIMB 13064 shows that the overall mechanisms are simi (en)
- Haloalkane dehalogenases are bacterial enzymes capable of carbon-halogen bond cleavage in halogenated compounds. To obtain insight in the mechanism of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB), we studied the steady-state and pre-steady-state kinetics of the conversion of the substrates 1-chlorohexane, chlorocyclohexane and bromocyclohexane. The results lead to a proposal of a minimal kinetic mechanism consisting of three main steps: (i) substrate binding, (ii) cleavage of the carbon-halogen bond with simultaneous formation of an alkyl-enzyme intermediate and (iii) hydrolysis of the alkyl-enzyme intermediate. Release of both products, halide and alcohol, is a fast process that was not included in reaction mechanism as a distinct step. Comparison of the kinetic mechanism of LinB with that of haloalkane dehalogenase DhlA from Xantobacter autotrophicus GJ10 and the haloalkane dehalogenase DhaA from Rhodococcus rhodochrous NCIMB 13064 shows that the overall mechanisms are simi (cs)
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| Title
| - Catalytic mechanism of the haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26
- Catalytic mechanism of the haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26 (en)
- Catalytic mechanism of the haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26 (cs)
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| skos:prefLabel
| - Catalytic mechanism of the haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26
- Catalytic mechanism of the haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26 (en)
- Catalytic mechanism of the haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26 (cs)
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| skos:notation
| - RIV/00216224:14310/03:00009155!RIV08-MSM-14310___
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| http://linked.open.../vavai/riv/strany
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
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| http://linked.open...ai/riv/idVysledku
| - RIV/00216224:14310/03:00009155
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| http://linked.open...riv/jazykVysledku
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| http://linked.open.../riv/klicovaSlova
| - ENZYME; KINETICS; MECHANISM; LINB; HALOALKANE DEHALOGENASE (en)
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| http://linked.open.../riv/klicoveSlovo
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| http://linked.open...odStatuVydavatele
| - US - Spojené státy americké
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| http://linked.open...ontrolniKodProRIV
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| http://linked.open...i/riv/nazevZdroje
| - Journal of Biological Chemistry
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| http://linked.open...in/vavai/riv/obor
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| http://linked.open...ichTvurcuVysledku
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| http://linked.open...cetTvurcuVysledku
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| http://linked.open...vavai/riv/projekt
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| http://linked.open...UplatneniVysledku
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| http://linked.open...v/svazekPeriodika
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| http://linked.open...iv/tvurceVysledku
| - Chaloupková, Radka
- Damborský, Jiří
- Klvaňa, Martin
- Nagata, Yuji
- Prokop, Zbyněk
- Monincová, Marta
- Janssen, Dick B.
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| number of pages
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| http://localhost/t...ganizacniJednotka
| |
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