The Effect of a Unique Halide-Stabilising Residue on the Catalytic Properties of Haloalkane Dehalogenase DatA from Agrobacterium tumefaciens C58
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F13%3A00065822" target="_blank" >RIV/00216224:14310/13:00065822 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1111/febs.12238" target="_blank" >http://dx.doi.org/10.1111/febs.12238</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/febs.12238" target="_blank" >10.1111/febs.12238</a>
Alternative languages
Result language
angličtina
Original language name
The Effect of a Unique Halide-Stabilising Residue on the Catalytic Properties of Haloalkane Dehalogenase DatA from Agrobacterium tumefaciens C58
Original language description
Haloalkane dehalogenases catalyse the hydrolysis of carbon-halogen bonds in various chlorinated, brominated and iodinated compounds. These enzymes have a conserved pair of halide-stabilising residues that are important in substrate binding and stabilisation of the transition state and the halide ion product via hydrogen bonding. In all previously known haloalkane dehalogenase, these residues are either a pair of tryptophans or a tryptophan-asparagine pair. The newly isolated haloalkane dehalogenase DatAfrom Agrobacterium tumefaciens C58 possesses a unique halide-stabilising tyrosine residue, Y109, in place of the conventional tryptophan. A variant of DatA with the Y109W mutation was created and the effects of this mutation on the enzyme?s structure and catalytic properties were studied using spectroscopy and pre-steady-state kinetic experiments.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FEBS Journal
ISSN
1742-464X
e-ISSN
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Volume of the periodical
280
Issue of the periodical within the volume
13
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
3149-3159
UT code for WoS article
000320557100016
EID of the result in the Scopus database
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