PAVLOVÁ, Martina, Martin KLVAŇA, Andrea JESENSKÁ, Zbyněk PROKOP, Hana KONEČNÁ, Yukari SATO, M. TSUDA, Yuji NAGATA and Jiří DAMBORSKÝ. The Identification of Catalytic Pentad in the Haloalkane Dehalogenase DhmA from Mycobacterium avium N85: Reaction Mechanism and Molecular Evolution. Journal of Structural Biology. 2007, vol. 157, No 2, p. 384-392. ISSN 1047-8477.
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Basic information
Original name The Identification of Catalytic Pentad in the Haloalkane Dehalogenase DhmA from Mycobacterium avium N85: Reaction Mechanism and Molecular Evolution
Name in Czech Identifikace katalytickych pentad v haloalkán dehalogenaze DhmA z kmene Mycobacterium avium N85: Reakční mechanismus a molekulární evoluce.
Authors PAVLOVÁ, Martina (203 Czech Republic), Martin KLVAŇA (203 Czech Republic), Andrea JESENSKÁ (203 Czech Republic), Zbyněk PROKOP (203 Czech Republic), Hana KONEČNÁ (203 Czech Republic), Yukari SATO (392 Japan), M. TSUDA (392 Japan), Yuji NAGATA (392 Japan) and Jiří DAMBORSKÝ (203 Czech Republic, guarantor).
Edition Journal of Structural Biology, 2007, 1047-8477.
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: 3.677
RIV identification code RIV/00216224:14310/07:00022383
Organization unit Faculty of Science
UT WoS 000243951800010
Keywords in English Catalytic Pentad; Haloalkane Dehalogenase; DhmA Mycobacterium avium N85
Tags Catalytic Pentad, DhmA Mycobacterium avium N85, haloalkane dehalogenase
Tags International impact, Reviewed
Changed by Changed by: prof. Mgr. Jiří Damborský, Dr., učo 1441. Changed: 22/3/2010 09:10.
Abstract
Haloalkane dehalogenase DhmA from Mycobacterium avium N85 showed poor expression and low stability when produced in Escherichia coli. Here we present expression DhmA in newly constructed pK4RP rhodococcal expression system in a soluble and stable form. Site-directed mutagenesis was used for the identification of a catalytic pentad, which makes up the reaction machinery of all currently known haloalkane dehalogenases. The putative catalytic triad Asp123, His279, Asp250 and the first halide-stabilizing residue Trp124 were deduced from sequence comparisons. The second stabilizing residue Trp164 was predicted from a homology model. Five point mutants in the catalytic pentad were constructed, tested for activity and were found inactive. A two-step reaction mechanism was proposed for DhmA. Evolution of different types of catalytic pentads and molecular adaptation towards the synthetic substrate 1,2-dichloroethane within the protein family is discussed.
Abstract (in Czech)
v clanku jsou popsany experimenty s Haloalkan dehalogenázou DhmA z bakterie Mycobacterium avium N85.
Links
MSM0021622413, plan (intention)Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
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