Since 1991, when the first haloalkane dehalogenase (HLD) from Xanthobacter autotrophicus GJ10 was described, nearly 20 HLDs have been characterized biochemically and fourteen HLDs were analysed structurally. These enzymes belong to alpha/beta-hydrolases and, owing to their ability to bring about the hydrolytic conversion of toxic halogenated compounds, are a source of broad biotechnological applications. DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marinobacter sp. ELB17 are among them. Although their overall structures are quite similar to other HLD members, they possess several unique properties. Information on their 3D structure may significantly contribute to the understanding of protein function. DpcA and DmxA structures will allow us to gain insights into structural determinants of specificity and stability. This thesis aims to elucidate the tertiary and quaternary structures of these enzymes using of X-ray crystallography.
| Identifer | oai:union.ndltd.org:nusl.cz/oai:invenio.nusl.cz:395949 |
| Date | January 2019 |
| Creators | DOLEŽELOVÁ, Katsiaryna |
| Source Sets | Czech ETDs |
| Language | English |
| Detected Language | English |
| Type | info:eu-repo/semantics/doctoralThesis |
| Rights | info:eu-repo/semantics/restrictedAccess |
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