Cloning, expression and preliminary characterization of novel haloalkane dehalogenase DhmA from Mycobacterium avium N85

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F02%3A00006277" target="_blank" >RIV/00216224:14310/02:00006277 - 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

Cloning, expression and preliminary characterization of novel haloalkane dehalogenase DhmA from Mycobacterium avium N85

Popis výsledku v původním jazyce

Haloalkane dehalogenases are microbial enzymes catalyzing the cleavage of carbon-halogen bond by a hydrolytic mechanism. Until recently, these enzymes have only been isolated from bacteria living in contaminated environments. This report describes the cloning of dehalogenase gene gene dhmA from Mycobacterium avium subsp. avium N85 isolated from swines mesenteric lymph node. The dhmA gene has G+C content 68.21 % and codes for a polypeptide 301 amino acids long with calculated molecular mass of 34.7 kDa.The molecular mass of DhmA determined by SDS electrophoresis and gel permeation chromatography is 34.0 and 35.4 kDa, respectively. Many residues essential for dehalogenation reaction are conserved in DhmA, i.e. the putative catalytic triad consists of Asp123, His279 and Asp250; the putative oxyanion hole is made of Glu55 and Trp124. Trp124 should be involved in substrate binding and product (halide) stabilization while the second halide stabilising residue cannot be identified from compa

Název v anglickém jazyce

Cloning, expression and preliminary characterization of novel haloalkane dehalogenase DhmA from Mycobacterium avium N85

Popis výsledku anglicky

Haloalkane dehalogenases are microbial enzymes catalyzing the cleavage of carbon-halogen bond by a hydrolytic mechanism. Until recently, these enzymes have only been isolated from bacteria living in contaminated environments. This report describes the cloning of dehalogenase gene gene dhmA from Mycobacterium avium subsp. avium N85 isolated from swines mesenteric lymph node. The dhmA gene has G+C content 68.21 % and codes for a polypeptide 301 amino acids long with calculated molecular mass of 34.7 kDa.The molecular mass of DhmA determined by SDS electrophoresis and gel permeation chromatography is 34.0 and 35.4 kDa, respectively. Many residues essential for dehalogenation reaction are conserved in DhmA, i.e. the putative catalytic triad consists of Asp123, His279 and Asp250; the putative oxyanion hole is made of Glu55 and Trp124. Trp124 should be involved in substrate binding and product (halide) stabilization while the second halide stabilising residue cannot be identified from compa

Druh

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

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A016" target="_blank" >LN00A016: BIOMOLEKULÁRNÍ CENTRUM</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2002

Kód důvěrnosti údajů

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

Název periodika

Applied and Environmental Microbiology

ISSN

1098-5336

e-ISSN

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Svazek periodika

68

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

3730

Strana od-do

3724

Kód UT WoS článku

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EID výsledku v databázi Scopus

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