| Attributes | Values |
|---|
| rdf:type
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| Description
| - Structural comparison of three different haloalkane dehalogenases suggested that substrate specificity of these bacterial enzymes could be significantly influenced by the size and shape of their entrance tunnels. The surface residue leucine 177 positioned at the tunnel opening of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26 was selected for modification based on structural and phylogenetic analysis: the residue partially blocks the entrance tunnel and it is the most variable pocket residue in haloalkane dehalogenase-like proteins with nine substitutions in fourteen proteins. Mutant genes coding for proteins carrying all possible substitutions in position 177 were constructed by site-directed mutagenesis and heterologously expressed in Escherichia coli. In total, fifteen active protein variants were obtained suggesting a relatively high tolerance of the site for the introduction of mutations. Purified protein variants were kinetically characterised by determination of specific activi
- Structural comparison of three different haloalkane dehalogenases suggested that substrate specificity of these bacterial enzymes could be significantly influenced by the size and shape of their entrance tunnels. The surface residue leucine 177 positioned at the tunnel opening of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26 was selected for modification based on structural and phylogenetic analysis: the residue partially blocks the entrance tunnel and it is the most variable pocket residue in haloalkane dehalogenase-like proteins with nine substitutions in fourteen proteins. Mutant genes coding for proteins carrying all possible substitutions in position 177 were constructed by site-directed mutagenesis and heterologously expressed in Escherichia coli. In total, fifteen active protein variants were obtained suggesting a relatively high tolerance of the site for the introduction of mutations. Purified protein variants were kinetically characterised by determination of specific activi (en)
- Structural comparison of three different haloalkane dehalogenases suggested that substrate specificity of these bacterial enzymes could be significantly influenced by the size and shape of their entrance tunnels. The surface residue leucine 177 positioned at the tunnel opening of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26 was selected for modification based on structural and phylogenetic analysis: the residue partially blocks the entrance tunnel and it is the most variable pocket residue in haloalkane dehalogenase-like proteins with nine substitutions in fourteen proteins. Mutant genes coding for proteins carrying all possible substitutions in position 177 were constructed by site-directed mutagenesis and heterologously expressed in Escherichia coli. In total, fifteen active protein variants were obtained suggesting a relatively high tolerance of the site for the introduction of mutations. Purified protein variants were kinetically characterised by determination of specific activi (cs)
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| Title
| - Modification of Activity and Specificity of Haloalkane Dehalogenase from Sphingomonas paucimobilis UT26 by Engineering of its Entrance Tunnel
- Modification of Activity and Specificity of Haloalkane Dehalogenase from Sphingomonas paucimobilis UT26 by Engineering of its Entrance Tunnel (en)
- Modification of Activity and Specificity of Haloalkane Dehalogenase from Sphingomonas paucimobilis UT26 by Engineering of its Entrance Tunnel (cs)
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| skos:prefLabel
| - Modification of Activity and Specificity of Haloalkane Dehalogenase from Sphingomonas paucimobilis UT26 by Engineering of its Entrance Tunnel
- Modification of Activity and Specificity of Haloalkane Dehalogenase from Sphingomonas paucimobilis UT26 by Engineering of its Entrance Tunnel (en)
- Modification of Activity and Specificity of Haloalkane Dehalogenase from Sphingomonas paucimobilis UT26 by Engineering of its Entrance Tunnel (cs)
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| skos:notation
| - RIV/00216224:14310/03:00009370!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
| |
| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
| |
| http://linked.open...iv/duvernostUdaju
| |
| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
| |
| http://linked.open...ai/riv/idVysledku
| - RIV/00216224:14310/03:00009370
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| http://linked.open...riv/jazykVysledku
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| http://linked.open.../riv/klicovaSlova
| - DEHALOGENASE MUTAGENESIS SPECIFICITY (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
| |
| http://linked.open...i/riv/nazevZdroje
| - Journal of Biological Chemistry
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| http://linked.open...in/vavai/riv/obor
| |
| http://linked.open...ichTvurcuVysledku
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| http://linked.open...cetTvurcuVysledku
| |
| http://linked.open...vavai/riv/projekt
| |
| http://linked.open...UplatneniVysledku
| |
| http://linked.open...v/svazekPeriodika
| |
| http://linked.open...iv/tvurceVysledku
| - Chaloupková, Radka
- Damborský, Jiří
- Fořtová, Andrea
- Nagata, Yuji
- Pavlová, Martina
- Prokop, Zbyněk
- Sýkorová, Jana
- Monincová, Marta
- Tsuda, Masataka
|
| issn
| |
| number of pages
| |
| http://localhost/t...ganizacniJednotka
| |
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