MAREK, Jaromír, Jitka VÉVODOVÁ, Ivana KUTÁ-SMATANOVÁ, Y. NAGATA, L.A. SVENSSON, J. NEWMAN, M. TAKAGI a Jiří DAMBORSKÝ. Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26. Biochemistry. Washington, DC, USA: American Chemical Society, 2000, roč. 39, č. 46, s. 14082-14086. ISSN 0006-2960. |
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@article{342723, author = {Marek, Jaromír and Vévodová, Jitka and KutáandSmatanová, Ivana and Nagata, Y. and Svensson, L.A. and Newman, J. and Takagi, M. and Damborský, Jiří}, article_location = {Washington, DC, USA}, article_number = {46}, keywords = {Crystal structure; haloalkane dehalogenase}, language = {eng}, issn = {0006-2960}, journal = {Biochemistry}, title = {Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26}, url = {http://www.ncbr.chemi.muni.cz/~jiri/ABSTRACTS/biochem00.html}, volume = {39}, year = {2000} }
TY - JOUR ID - 342723 AU - Marek, Jaromír - Vévodová, Jitka - Kutá-Smatanová, Ivana - Nagata, Y. - Svensson, L.A. - Newman, J. - Takagi, M. - Damborský, Jiří PY - 2000 TI - Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26 JF - Biochemistry VL - 39 IS - 46 SP - 14082 EP - 14082 PB - American Chemical Society SN - 00062960 KW - Crystal structure KW - haloalkane dehalogenase UR - http://www.ncbr.chemi.muni.cz/~jiri/ABSTRACTS/biochem00.html N2 - The haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB) is the enzyme involved in the degradation ofthe important environmental pollutant g-hexachlorocyclohexane. The enzyme hydrolyzes a broad range of halogenated cyclic and aliphatic compounds. Here, we present the 1.58 A crystal structure of LinB and the 2.0 A structure of LinB with 1,3-propanediol, a product of debromination of 1,3-dibromopropane, in the active site of the enzyme. The enzyme belongs to the a/b-hydrolase family and contains a catalytic triad (Aspl08, His272, and Glu132) in the lipase-like topological arrangement previously proposed from mutagenesis experiments. The LinB structure was compared with the structures of haloalkane dehalogenase from Xanthobacter autotrophicus GJl0 and from Rhodococcus sp. and the structural features involved in the adaptation toward xenobiotic substrates were identified. The arrangement and composition of the a-helices in the cap domain results in the dif ferences in the size and shape of the active-site cavity and the entrance tunnel. This is the major determinant ofthe substrate specificity ofthis haloalkane dehalogenase. ER -
MAREK, Jaromír, Jitka VÉVODOVÁ, Ivana KUTÁ-SMATANOVÁ, Y. NAGATA, L.A. SVENSSON, J. NEWMAN, M. TAKAGI a Jiří DAMBORSKÝ. Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26. \textit{Biochemistry}. Washington, DC, USA: American Chemical Society, 2000, roč.~39, č.~46, s.~14082-14086. ISSN~0006-2960.
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