Substrate specificity of haloalkane dehalogenases

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00009966" target="_blank" >RIV/00216224:14310/04:00009966 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Substrate specificity of haloalkane dehalogenases
Original language description
Haloalkane dehalogenases are microbial enzymes capable to cleave carbon-halogen bond in halogenated aliphatic compounds. There is a growing interest in these enzymes because of their potential use in bioremediation, as industrial biocatalysts, or as biosensors. Structurally, haloalkane dehalogenases belong to the a/b-hydrolase fold superfamily. Best studied haloalkane dehalogeneses are DhlA from Xanthobacter autotrophicus GJ10 [1], DhaA from Rhodococcus rhodochrous NCIMB 13064 [2] and LinB from Sphingomonas paucimobilis UT26 [3]. Crystal structures of these haloalkane dehalogenases are known. There is a number of DNA sequences which are expected to code haloalkane dehalogenases. This expectation is based on sequential similiraties with known haloalkanedehalogenases: DhlA, DhaA and LinB. Protein Rv2579 from Mycobacterium tuberculosis H37Rv has 68 % sequence similarity with LinB. Gene rv2579 was cloned to Escherichia coli, protein Rv2579 was overexpressed and purified to homogeneity. Ha
Czech name
Substratová specifita haloalkán dehalogenáz.
Czech description
haloalkan dehalogenázy jsou mikrobiální enzymy schopné štípat vazbu uhlík-vodík v halogenovaných alifatických sloučeninách. V práci byly měřena rozdíly aktivit u různých substrátů.

Project
<a href="/en/project/LN00A016" target="_blank" >LN00A016: BIOMOLECULAR CENTER</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2004
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Article name in the collection
Materials Structure in Chemistry, Biology, Physics and Technology
ISBN
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ISSN
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e-ISSN
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Number of pages
2
Pages from-to
32-33
Publisher name
Czech and Slovak Crystallographic Association
Place of publication
Praha
Event location
Univerzitní a akademické centrum Nové Hrady
Event date
Mar 11, 2004
Type of event by nationality
CST - Celostátní akce
UT code for WoS article
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