NAGATA, Yuji, Zbyněk PROKOP, Soňa MARVANOVÁ, Jana SÝKOROVÁ, Marta MONINCOVÁ, Masataka TSUDA and Jiří DAMBORSKÝ. Re-construction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB. Applied and Environmental Microbiology. 2003, vol. 69, No 4, p. 2349-2355. ISSN 1098-5336.
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Basic information
Original name Re-construction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB
Name in Czech Re-konstrukce mycobakteriální dehalogenázy Rv2579 kumulativní mutagenezí haloalkán dehalogenázy LinB
Authors NAGATA, Yuji (392 Japan), Zbyněk PROKOP (203 Czech Republic), Soňa MARVANOVÁ (203 Czech Republic), Jana SÝKOROVÁ (203 Czech Republic), Marta MONINCOVÁ (203 Czech Republic), Masataka TSUDA (392 Japan) and Jiří DAMBORSKÝ (203 Czech Republic, guarantor).
Edition Applied and Environmental Microbiology, 2003, 1098-5336.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 3.820
RIV identification code RIV/00216224:14310/03:00009851
Organization unit Faculty of Science
UT WoS 000182151800061
Keywords in English MUTANT; EVOLUTION; MYCOBACTERIUM; DEHALOGENATION; BIODEGRADATION
Tags biodegradation, dehalogenation, Evolution, MUTANT, MYCOBACTERIUM
Changed by Changed by: prof. Mgr. Jiří Damborský, Dr., učo 1441. Changed: 19/3/2010 11:05.
Abstract
The homology model of protein Rv2579 from Mycobacterium tuberculosis H37Rv was compared with the crystal structure of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26 and uncovered that six out of nineteen amino acid residues which form an active site and entrance tunnel are different between LinB and Rv2579. To characterize an effect of replacements of these six amino acid residues, mutations were introduced cumulatively into the six amino acid residues of LinB. The six-fold mutant which is supposed to have an active site of Rv2579 showed haloalkane dehalogenase activity with tested haloalkanes, confirming that Rv2579 is a member of haloalkane dehalogenase protein family.
Abstract (in Czech)
Model proteinu Rv2579 z bakterie Mycobacretium tuberculosis byl srovnán s krystalovou strukturou haloalkán dehalogenázy LinB z bakterie Sphingomonas paucimobilis.
Links
LN00A016, research and development projectName: BIOMOLEKULÁRNÍ CENTRUM
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular Center
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