Mykobakteriální haloalkán dehalogenázy:klonování, biochemické vlastnosti a distribuce.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F05%3A00014724" target="_blank" >RIV/00216224:14310/05:00014724 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Mycobacterial Haloalkane Dehalogenases: Cloning, Biochemical Properties and distribution.

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

Mycobacterial Haloalkane Dehalogenases: Cloning, Biochemical Properties and distribution.

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2005

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Applied and Environmental Microbiology

ISSN

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e-ISSN

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Svazek periodika

71

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

6736-6745

Kód UT WoS článku

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EID výsledku v databázi Scopus

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