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Structure-activity investigation on laccases by computational and site directed mutagenesis studies

Author
Delavari, A.
Type of activity
Theses
Other related units
Department of Agri-Food Engineering and Biotechnology
Defense's date
2016-12-01
URL
http://hdl.handle.net/2117/106481 Open in new window
Abstract
Laccases belong to multi copper oxidase enzyme family (EC 1.10.3.2). Their capacity to oxidíze a wide range of substrates makes them very attractive for the industry and are growing in importance for environmentally-friendly synthesis. Laccases have three different copper sites including, type 1 (T1), type 2 (T2) and type 3 (T3). The function of the T1 site is shuttling electrons from the substrate to the trinuclear copper cluster. During the catalytic cycle of laccase, four electrons are remo...
Group of research
CEBIM - Molecular Biotechnology Centre
GBMI - Molecular and Industrial Biotechnology Group
Citation
Delavari, A. "Structure-activity investigation on laccases by computational and site directed mutagenesis studies". Tesi doctoral, UPC, Departament d'Enginyeria Agroalimentària i Biotecnologia, 2016.

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