English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/10376
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


Characterization of the endo-β-1,3-glucanase activity of S. cerevisiae Eng2 and other members of the GH81 family

AuthorsMartín-Cuadrado, Ana Belén; Esteban, Pedro Felipe; Encinar del Dedo, Javier ; Medina-Redondo, María de ; Rey Iglesias, Francisco del ; Vázquez de Aldana, Carlos R.
Glycoside hydrolase
Catalytic domain
Active site
Issue DateApr-2008
CitationFungal Genetics and Biology 45(4): 542-553 (2008)
AbstractThe GH81 family includes proteins with endo-β-1,3-glucanase widely distributed in yeast and fungi, which are also present in plants and bacteria. We have studied the activity of the Saccharomyces cerevisiae ScEng2 and the Schizosaccharomyces pombe SpEng1 and SpEng2 proteins. All three proteins exclusively hydrolyzed linear β-1,3-glucan chains. Laminari-oligosaccharide degradation revealed that the minimum substrate length that the three endoglucanases were able to efficiently degrade was a molecule with at least 5 glucose residues, suggesting that the active site of the enzymes recognized five glucose units. Prediction of the secondary structure of ScEng2 and comparison with proteins of known structure allowed the identification of a 404-amino acid region with a structure similar to the Clostridium thermocellum endoglucanase CelA. This fragment showed similar enzymatic characteristics to those of the complete protein, suggesting that it contains the catalytic domain of this family of proteins. Within this domain, four conserved Asp and Glu residues (D518, D588, E609, and E613) are necessary for enzymatic activity.
Description12 pages, 6 figures.-- et al.
Publisher version (URL)http://dx.doi.org/10.1016/j.fgb.2007.09.001
Appears in Collections:(IMB) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

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