English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/133217
Share/Impact:
Statistics
logo share SHARE   Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Title

Molecular determinants for selective C25-hydroxylation of vitamins D2 and D3 by fungal peroxygenases

AuthorsCañellas, Marina; Lucas, Fátima; Babot, Esteban Daniel ; Río Andrade, José Carlos del ; Kalum, Lisbeth; Ullrich, René; Hofrichter, Martin; Guallar, Victor; Martínez, Ángel T. ; Gutiérrez Suárez, Ana
Issue Date1-Oct-2015
PublisherUniversidad de Barcelona
Citation4th New Trends in Computational Chemistry for Industrial Applications Póster 7 (2015)
AbstractSelective oxygenations of aliphatic compounds are among the most challenging reactions in organic chemistry for the regio and/or stereo specific synthesis of pharmaceuticals and fine chemicals. Recently, a new peroxidase type, which shares the active-site architecture and reaction mechanism of cytochromes P450, but has the advantage of being activated directly by H2O2, was isolated from Agrocybe aegerita (Ullrich, 2004), and later identified in a variety of sequenced basidiomycete genomes, including that of Coprinopsis cinerea (Floudas, 2012). The A. aegerita heme-thiolate (HTP) enzyme has been the most widely investigated basidiomycete peroxygenase, and recent studies have shown that the C. cinerea enzyme has comparative advantages related to its high conversion yield/selectivity for some hydroxylation reactions, and its production as a recombinant protein in an industrial expression host (Babot, 2013; 2014). 25-monohydroxylated vitamin D3 (cholecalciferol) and D2 (ergocalciferol), compounds of high interest in human health and animal feeding, can be obtained through reaction with both A. aegerita and C. cinerea enzymes. In the present study, PELE computational analyses are used to rationalize the underlying mechanisms responsible for differences in reactivity and selectivity observed experimentally between both enzymes (Lucas, 2015). References Babot, E. D., et al., Biotechnol. Bioeng., (2013), 110, 2332. Babot, E. D., et al., Chemcatchem, (2014), online. Floudas, D., et al. Science, (2012), 336, 1715-1719. Lucas, F., et al. Catal. Sci. Tech., (2015), online. Ullrich, R., et al., Appl. Environ. Microbiol. (2004), 70, 4575-4581.
DescriptionPoster nº 7 presentado en el 4th New Trends in Computational Chemistry for Industrial Applications 1-2 Octubre, Barcelona (2015)
Publisher version (URL)http://www.xrqtc.com/workshop2015/wp-content/uploads/sites/2/2015/05/POSTER-SESSION.pdf
URIhttp://hdl.handle.net/10261/133217
Appears in Collections:(IRNAS) Comunicaciones congresos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.