Slabá aktivita haloalkan dehalogenázy LinB s 1,2,3-Trichloropropanem srovnávání pomocí X-ray Krystalografie a Microkalorimetrie.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F07%3A00022815" target="_blank" >RIV/00216224:14310/07:00022815 - 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

Weak Activity of Haloalkane Dehalogenase LinB with 1,2,3-Trichloropropane Revealed by X-ray Crystallography and Microcalorimetry

Popis výsledku v původním jazyce

,2,3-trichloropropane (TCP) is a highly toxic and recalcitrant compound. Haloalkane dehalogenases are bacterial enzymes catalysing the cleavage of a carbon-halogen bond in a wide range of organic halogenated compounds. Haloalkane dehalogenase LinB from Sphingobium japonicum UT26 has, for a long time, been considered inactive with TCP since the reaction can not be easily detected by conventional analytical methods. Here we demonstrate detection of the weak activity (kcat = 0.005 s-1) of LinB with TCP using X-ray crystallography and microcalorimetry. This observation makes LinB a useful starting material for development of new biocatalyst towards TCP by protein engineering. Microcalorimetry is proposed to be a universal method for detection of weak enzymatic activities. Detection of these activities is becoming increasingly important for engineering of novel biocatalysts using the scaffolds of proteins with promiscuous activities.

Název v anglickém jazyce

Weak Activity of Haloalkane Dehalogenase LinB with 1,2,3-Trichloropropane Revealed by X-ray Crystallography and Microcalorimetry

Popis výsledku anglicky

,2,3-trichloropropane (TCP) is a highly toxic and recalcitrant compound. Haloalkane dehalogenases are bacterial enzymes catalysing the cleavage of a carbon-halogen bond in a wide range of organic halogenated compounds. Haloalkane dehalogenase LinB from Sphingobium japonicum UT26 has, for a long time, been considered inactive with TCP since the reaction can not be easily detected by conventional analytical methods. Here we demonstrate detection of the weak activity (kcat = 0.005 s-1) of LinB with TCP using X-ray crystallography and microcalorimetry. This observation makes LinB a useful starting material for development of new biocatalyst towards TCP by protein engineering. Microcalorimetry is proposed to be a universal method for detection of weak enzymatic activities. Detection of these activities is becoming increasingly important for engineering of novel biocatalysts using the scaffolds of proteins with promiscuous activities.

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

2007

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

73

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

4

Strana od-do

2005-2008

Kód UT WoS článku

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EID výsledku v databázi Scopus

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