Identification of protein fold and catalytic residues of g-hexachlorocyclohexane dehydrochlorinase LinA

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F01%3A00005567" target="_blank" >RIV/00216224:14310/01:00005567 - 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

Identification of protein fold and catalytic residues of g-hexachlorocyclohexane dehydrochlorinase LinA

Popis výsledku v původním jazyce

g-Hexachlorocyclohexane dehydrochlorinase (LinA) is a unique dehydrochlorinase that has no homologous sequence at the amino acid-sequence level, and for which the evolutionary origin is unknown. We here propose that LinA is a member of a novel structuralsuperfamily of enzymes containing scytalone dehydratase, 3-oxo-D5-steroid isomerase, nuclear transport factor-2, and the b-subunit of naphthalene dioxygenase-all known structures with different functions. The catalytic and the active site residues of LinA are predicted based on its homology model. Nine mutants that carry substitutions in the proposed catalytic residues were constructed by site-directed mutagenesis. In addition to these, eight mutants that have a potential to make contact with the substrate were prepared by site-directed mutagenesis. These mutants were expressed in E. coli, and their activities in crude extract were evaluated. Most of the features of the LinA mutants could be explained on the basis of the present LinA m

Název v anglickém jazyce

Identification of protein fold and catalytic residues of g-hexachlorocyclohexane dehydrochlorinase LinA

Popis výsledku anglicky

g-Hexachlorocyclohexane dehydrochlorinase (LinA) is a unique dehydrochlorinase that has no homologous sequence at the amino acid-sequence level, and for which the evolutionary origin is unknown. We here propose that LinA is a member of a novel structuralsuperfamily of enzymes containing scytalone dehydratase, 3-oxo-D5-steroid isomerase, nuclear transport factor-2, and the b-subunit of naphthalene dioxygenase-all known structures with different functions. The catalytic and the active site residues of LinA are predicted based on its homology model. Nine mutants that carry substitutions in the proposed catalytic residues were constructed by site-directed mutagenesis. In addition to these, eight mutants that have a potential to make contact with the substrate were prepared by site-directed mutagenesis. These mutants were expressed in E. coli, and their activities in crude extract were evaluated. Most of the features of the LinA mutants could be explained on the basis of the present LinA m

Druh

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

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

2001

Kód důvěrnosti údajů

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

Název periodika

PROTEINS: Structure, Function, and Genetics

ISSN

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e-ISSN

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Svazek periodika

45

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

7

Strana od-do

471

Kód UT WoS článku

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EID výsledku v databázi Scopus

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