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

Result code in 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>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Beta-Galactosidase from Antarctic bacterium Arthrobacter sp. C2-2: a molecular modelling study
Original language description
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
Czech name
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Czech description
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Project
<a href="/en/project/GA204%2F02%2F0843" target="_blank" >GA204/02/0843: Complex cold adaptation study of enzymes on molecular level and their application in biotechnology</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2003
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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