Rekonstrukce mykobakterialního proteinu Rv2579 v haloalkán dehalogezáze Lin B z bakterie Sphingomonas paucimobilis UT26

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00025489" target="_blank" >RIV/00216224:14310/04:00025489 - 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

Reconstruction of Mycobacterial Protein Rv2579 in Haloalkane Dehalogenase LinB from Sphingomonas paucimobilis UT26

Popis výsledku v původním jazyce

Gene rv2579 was found in complete genome sequence of Mycobacterium tuberculosis H37Rv and was supposed to code haloalkane dehalogenase due to 68% sequence identity with LinB which is haloalkane dehalogenase from Sphingomonas paucimobilis UT26 [1]. Objective of the study was to test membership of Rv2579 protein within haloalkane dehalogenase family. The homology model of protein Rv2579 was compared with the crystal structure of haloalkane dehalogenase LinB [2]. This analysis revealed that 6 out of 19 amino acid residues which form an active site and entrance tunnel are different in LinB and Rv2579. The 6 different amino acids were cumulatively mutated in LinB. Final six-fold mutant was presumed to have active site and entrance tunnel of Rv2579 and exhibited dehalogenase activity with the haloalkanes tested, confirming that Rv2579 is a member of the haloalkane dehalogenase family [3]. Consequently the rv2579 gene was cloned from Mycobacterium bovis 5032/66 into Escherichia coli. Rv2579 p

Název v anglickém jazyce

Reconstruction of Mycobacterial Protein Rv2579 in Haloalkane Dehalogenase LinB from Sphingomonas paucimobilis UT26

Popis výsledku anglicky

Gene rv2579 was found in complete genome sequence of Mycobacterium tuberculosis H37Rv and was supposed to code haloalkane dehalogenase due to 68% sequence identity with LinB which is haloalkane dehalogenase from Sphingomonas paucimobilis UT26 [1]. Objective of the study was to test membership of Rv2579 protein within haloalkane dehalogenase family. The homology model of protein Rv2579 was compared with the crystal structure of haloalkane dehalogenase LinB [2]. This analysis revealed that 6 out of 19 amino acid residues which form an active site and entrance tunnel are different in LinB and Rv2579. The 6 different amino acids were cumulatively mutated in LinB. Final six-fold mutant was presumed to have active site and entrance tunnel of Rv2579 and exhibited dehalogenase activity with the haloalkanes tested, confirming that Rv2579 is a member of the haloalkane dehalogenase family [3]. Consequently the rv2579 gene was cloned from Mycobacterium bovis 5032/66 into Escherichia coli. Rv2579 p

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

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

2004

Kód důvěrnosti údajů

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

Název statě ve sborníku

6th International Conference on Protein Stabilization

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

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Název nakladatele

Slovak Society of Chemical Engineering

Místo vydání

Bratislava, Slovakia

Místo konání akce

Bratislava

Datum konání akce

26. 9. 2004

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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