J 2005

Mycobacterial Haloalkane Dehalogenases: Cloning, Biochemical Properties and distribution.

JESENSKÁ, Andrea, Martina PAVLOVÁ, Michal STROUHAL, Radka CHALOUPKOVÁ, Iva TĚŠÍNSKÁ et. al.

Basic information

Original name

Mycobacterial Haloalkane Dehalogenases: Cloning, Biochemical Properties and distribution.

Name in Czech

Mykobakteriální haloalkán dehalogenázy:klonování, biochemické vlastnosti a distribuce.

Authors

JESENSKÁ, Andrea (203 Czech Republic), Martina PAVLOVÁ (203 Czech Republic), Michal STROUHAL (203 Czech Republic), Radka CHALOUPKOVÁ (203 Czech Republic), Iva TĚŠÍNSKÁ (203 Czech Republic), Marta MONINCOVÁ (203 Czech Republic), Zbyněk PROKOP (203 Czech Republic), Milan BARTOŠ (203 Czech Republic), Ivo PAVLÍK (203 Czech Republic), Ivan RYCHLÍK (203 Czech Republic), Petra MOBIUS (276 Germany), Yuji NAGATA (392 Japan) and Jiří DAMBORSKÝ (203 Czech Republic, guarantor)

Edition

Applied and Environmental Microbiology, 2005, 0099-2240

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

Impact factor

Impact factor: 3.818

RIV identification code

RIV/00216224:14310/05:00014724

Organization unit

Faculty of Science

UT WoS

000233225000035

Keywords in English

haloalkane dehalogenases; mycobacterium; cloning;

Tags

Změněno: 19/3/2010 12:17, prof. Mgr. Jiří Damborský, Dr.

Abstract

ORIG CZ

V originále

Haloalkane dehalogenases are enzymes catalysing the cleavage of the carbon-halogen bond by a hydrolytic mechanism. Genomes of Mycobacterium tuberculosis and M. bovis contain at least two open reading frames coding for the polypeptides showing a high sequence similarity with biochemically characterised haloalkane dehalogenases. In this paper we have described the cloning of the haloalkane dehalogenase genes dmbA and dmbB from M. bovis 5033/66 and proved the dehalogenase activity of their translation products. Both these genes are widely distributed among species of the M. tuberculosis complex, including M. bovis, M. bovis BCG, M. africanum, M. caprae, M. microti, and M. pinnipedii, as shown by the PCR screening of forty eight isolates from various hosts. DmbA and DmbB proteins were heterologously expressed in Escherichia coli and purified to homogeneity. The DmbB protein had to be expressed in a fusion with thioredoxin to obtain a soluble protein sample. The temperature optimum of DmbA and DmbB proteins determined with 1,2-dibromoethane is 45C. The melting temperature assessed by circular dichroism spectroscopy of DmbA is 47C and DmbB is 57C. The pH optimum of DmbA depends on composition of a buffer with maximal activity at 9.0. DmbB had a single pH optimum at pH 6.5. Mycobacteria are currently the only genus known to carry more than one haloalkane dehalogenase gene although putative haloalkane dehalogenases can be inferred in more then 20 different bacterial species by comparative genomics. Evolution and distribution of haloalkane dehalogenases among mycobacteria is discussed.

In Czech

Haloalán dehalogenázy jsou enzymy, katalyzující rozštěpení vazby C-H pomocí hydrolitického mechanismu. V článku je popisována studie genomů bakterií Mycobacterium tuberculosis a M. bovis. Jejich klonování, evoluce a distribuce.

Links

MSM0021622412, plan (intention)
Name: Interakce mezi chemickými látkami, prostředím a biologickými systémy a jejich důsledky na globální, regionální a lokální úrovni (INCHEMBIOL) (Acronym: INCHEMBIOL)
Investor: Ministry of Education, Youth and Sports of the CR, Interactions among the chemicals, environment and biological systems and their consequences on the global, regional and local scales (INCHEMBIOL)