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Strukturní studie halogenalkandehalogenasy DgaA z \kur{Glaciecola agarilytica} NO2
BERKOVÁ, Ivana
Haloalkane dehalogenases (HLDs) are microbial enzymes that have attracted significant interest because of their ability to catalyze the irreversible hydrolysis of a wide range of halogenated compounds. These enzymes can be used as potential applicants in industrial catalysis, in the bioremediation and the biosensing of environmental pollutants. Novel haloalkane dehalogenase DgaA (EC 3.8.1.5, HLDs) belonging to the superfamily of / hydrolases, was isolated from a psychrophilic and moderately halophilic organism, Glaciecola agarilytica NO2, that was found in marine sediment collected from the East Sea, Korea. Main target of this thesis was the processing of diffraction data from crystals of DgaA proteins and subsequent solving and refinement of structure of studied protein.
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Krystalizační studie nově izolované halogenalkandehalogenasy DgaA z \kur{Glacieocola agarilytica} NO2
BERKOVÁ, Ivana
This bachelors thesis is focused on crystalization study of newly prepared halogenalkanedehalogenase DgaA from bacteria Glaciecola agarylitica NO2. Main target of this work is getting acquianted with methods of protein crystalization and usage of those methods for preparation of suitable DgaA protein crystals of that will be used for X-ray structural analysis. Results from difraction analysis of DgaA crystals will be starting point for further research focused on structure determination and and description of protein function.
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Biodegradation of environmental pollutans - Crystallization haloalkan dehalogenase DpcA of Psychrobacter cryohalolentis K5
JUNG, Jakub
Knowledge of protein structures is necessary to clarify their structure-function relationships. Haloalkane dehalogenases are microbial enzymes that catalyze the hydrolysis of carbon-halogen in the halogenated hydrocarbons. Based on their properties these enzymes are able to degrade halogenated compounds. As the environment is burdened by a lot of different pollutants, biodegradation is a necessary step to improve the quality of environment. Haloalkane dehalogenases can be used as biosensors since they can detect contamination by halogenated compounds. This thesis is focused on crystallization of the model protein lysozyme and haloalkane dehalogenase DpcA isolated from the organism Psychrobacter cryohalolentis K5. The aim of this work was to prepare crystals suitable for X-ray diffraction analysis. After verification of protein?s purity, both proteins were crystallized by the use of basic and advanced crystallization methods. Single crystals of suitable size and quality for X-ray diffraction analysis were obtained and diffraction data were used to solve the 3D atomic structure of the DpcA. Since haloalkane dehalogenases have a low activity for halogenated substrates, the main aim of protein engineering is to increase their activity so thus further research is focused on modification of substrate specificity.
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