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

Result code in 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>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

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

Original language description

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

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EE - Microbiology, virology

OECD FORD branch

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Project

<a href="/en/project/LN00A016" target="_blank" >LN00A016: BIOMOLECULAR CENTER</a><br>

Continuities

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

Publication year

2002

Confidentiality

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

Name of the periodical

Applied and Environmental Microbiology

ISSN

1098-5336

e-ISSN

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Volume of the periodical

68

Issue of the periodical within the volume

8

Country of publishing house

US - UNITED STATES

Number of pages

3730

Pages from-to

3724

UT code for WoS article

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EID of the result in the Scopus database

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