Beta-Galactosidase from Antarctic bacterium Arthrobacter sp. C2-2: a molecular modelling study

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F03%3A00008978" target="_blank" >RIV/60461373:22330/03:00008978 - 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

Beta-Galactosidase from Antarctic bacterium Arthrobacter sp. C2-2: a molecular modelling study

Popis výsledku v původním jazyce

Enzymes from cold adapted microorganisms are being studied as potential catalysts in biotechnology as well as models of adaptation on an evolutionary level. The relationship between structural features of these enzymes and their ability to efficiently catalyse reactions at low temperatures is not clear. A study of beta-galactosidase from Antarctic bacteria Arthrobacter sp. C2-2 is presented. Model of 3D-structure of this enzyme was built using a methodology of homology modelling by satisfaction of spatial restraints based on structure of beta-galactosidase from E. coli (1DP0), the structure of one loop region was predicted ab initio. Interactions between the enzyme and ligands (galactose, water and ions) was studied using a methodology of molecular fields, docking, molecular dynamics simulation and free-energy scoring. Overall quality of the model was evaluated by 1 ns molecular dynamics simulation. We present comparison of structural features of the studied enzyme and its mesophilic c

Název v anglickém jazyce

Beta-Galactosidase from Antarctic bacterium Arthrobacter sp. C2-2: a molecular modelling study

Popis výsledku anglicky

Enzymes from cold adapted microorganisms are being studied as potential catalysts in biotechnology as well as models of adaptation on an evolutionary level. The relationship between structural features of these enzymes and their ability to efficiently catalyse reactions at low temperatures is not clear. A study of beta-galactosidase from Antarctic bacteria Arthrobacter sp. C2-2 is presented. Model of 3D-structure of this enzyme was built using a methodology of homology modelling by satisfaction of spatial restraints based on structure of beta-galactosidase from E. coli (1DP0), the structure of one loop region was predicted ab initio. Interactions between the enzyme and ligands (galactose, water and ions) was studied using a methodology of molecular fields, docking, molecular dynamics simulation and free-energy scoring. Overall quality of the model was evaluated by 1 ns molecular dynamics simulation. We present comparison of structural features of the studied enzyme and its mesophilic c

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA204%2F02%2F0843" target="_blank" >GA204/02/0843: Komplexní studium chladového přizpůsobení enzymů na molekulární úrovni a jejich uplatnění v biotechnologických procesech</a><br>

Návaznosti

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

Rok uplatnění

2003

Kód důvěrnosti údajů

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

Název statě ve sborníku

Sborník CUKRBLIK

ISBN

80-86238-30-2

ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

14

Název nakladatele

VŠCHT

Místo vydání

Praha

Místo konání akce

Praha

Datum konání akce

16. 4. 2003

Typ akce podle státní příslušnosti

CST - Celostátní akce

Kód UT WoS článku

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