Mycobacterial Haloalkane Dehalogenases: Cloning, Biochemical
Properties and distribution.

J 2005

Mycobacterial Haloalkane Dehalogenases: Cloning, Biochemical Properties and distribution.

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

Základní údaje

Originální název

Mycobacterial Haloalkane Dehalogenases: Cloning, Biochemical Properties and distribution.

Název česky

Mykobakteriální haloalkán dehalogenázy:klonování, biochemické vlastnosti a distribuce.

Autoři

JESENSKÁ, Andrea (203 Česká republika), Martina PAVLOVÁ (203 Česká republika), Michal STROUHAL (203 Česká republika), Radka CHALOUPKOVÁ (203 Česká republika), Iva TĚŠÍNSKÁ (203 Česká republika), Marta MONINCOVÁ (203 Česká republika), Zbyněk PROKOP (203 Česká republika), Milan BARTOŠ (203 Česká republika), Ivo PAVLÍK (203 Česká republika), Ivan RYCHLÍK (203 Česká republika), Petra MOBIUS (276 Německo), Yuji NAGATA (392 Japonsko) a Jiří DAMBORSKÝ (203 Česká republika, garant)

Vydání

Applied and Environmental Microbiology, 2005, 0099-2240

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.818

Kód RIV

RIV/00216224:14310/05:00014724

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000233225000035

Klíčová slova anglicky

haloalkane dehalogenases; mycobacterium; cloning;

Štítky

CLONING, Haloalkane dehalogenases, MYCOBACTERIUM

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

Anotace

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.

Česky

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.

Návaznosti

MSM0021622412, záměr

Název: Interakce mezi chemickými látkami, prostředím a biologickými systémy a jejich důsledky na globální, regionální a lokální úrovni (INCHEMBIOL) (Akronym: INCHEMBIOL)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Interakce mezi chemickými látkami, prostředím a biologickými systémy a jejich důsledky na globální , regionální a lokální úrovni

Citovat

JESENSKÁ, Andrea, Martina PAVLOVÁ, Michal STROUHAL, Radka CHALOUPKOVÁ, Iva TĚŠÍNSKÁ, Marta MONINCOVÁ, Zbyněk PROKOP, Milan BARTOŠ, Ivo PAVLÍK, Ivan RYCHLÍK, Petra MOBIUS, Yuji NAGATA a Jiří DAMBORSKÝ. Mycobacterial Haloalkane Dehalogenases: Cloning, Biochemical Properties and distribution. Applied and Environmental Microbiology. 2005, roč. 71, č. 11, s. 6736-6745. ISSN 0099-2240.

@article{620146,
   author = {Jesenská, Andrea and Pavlová, Martina and Strouhal, Michal and Chaloupková, Radka and Těšínská, Iva and Monincová, Marta and Prokop, Zbyněk and Bartoš, Milan and Pavlík, Ivo and Rychlík, Ivan and Mobius, Petra and Nagata, Yuji and Damborský, Jiří},
   article_number = {11},
   keywords = {haloalkane dehalogenases; mycobacterium; cloning;},
   language = {eng},
   issn = {0099-2240},
   journal = {Applied and Environmental Microbiology},
   title = {Mycobacterial Haloalkane Dehalogenases: Cloning, Biochemical Properties and distribution.},
   url = {http://loschmidt.chemi.muni.cz/peg/abstracts/aem05c.html},
   volume = {71},
   year = {2005}
}

TY  - JOUR
ID  - 620146
AU  - Jesenská, Andrea - Pavlová, Martina - Strouhal, Michal - Chaloupková, Radka - Těšínská, Iva - Monincová, Marta - Prokop, Zbyněk - Bartoš, Milan - Pavlík, Ivo - Rychlík, Ivan - Mobius, Petra - Nagata, Yuji - Damborský, Jiří
PY  - 2005
TI  - Mycobacterial Haloalkane Dehalogenases: Cloning, Biochemical Properties and distribution.
JF  - Applied and Environmental Microbiology
VL  - 71
IS  - 11
SP  - 6736-6745
EP  - 6736-6745
SN  - 00992240
KW  - haloalkane dehalogenases
KW  - mycobacterium
KW  - cloning;
UR  - http://loschmidt.chemi.muni.cz/peg/abstracts/aem05c.html
N2  - 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.
ER  -

JESENSKÁ, Andrea, Martina PAVLOVÁ, Michal STROUHAL, Radka CHALOUPKOVÁ, Iva TĚŠÍNSKÁ, Marta MONINCOVÁ, Zbyněk PROKOP, Milan BARTOŠ, Ivo PAVLÍK, Ivan RYCHLÍK, Petra MOBIUS, Yuji NAGATA a Jiří DAMBORSKÝ. Mycobacterial Haloalkane Dehalogenases: Cloning, Biochemical Properties and distribution. \textit{Applied and Environmental Microbiology}. 2005, roč.~71, č.~11, s.~6736-6745. ISSN~0099-2240.

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