tailieunhanh - Báo cáo khoa học: A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21

Approximately 10% of amylolytic enzymes are able to bind and degrade raw starch. Usually a distinct domain, the starch-binding domain (SBD), is responsible for this property. These domains have been classified into families of carbohydrate-binding modules (CBM). At present, there are six SBD families: CBM20, CBM21, CBM25, CBM26, CBM34, and CBM41. | ềFEBS Journal A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21 Martin Machovic1 Birte Svensson2 E. Ann MacGregor3 and Stefan Janecek1 1 Institute of Molecular Biology Slovak Academy of Sciences Bratislava Slovakia 2 Biochemistry and Nutrition Group BioCentrum-DTU TechnicalUniversity of Denmark Kgs. Lyngby Denmark 3 2 Nicklaus Green Livingston West Lothian UK Keywords carbohydrate-binding module evolutionary tree glycoside hydrolase family sequence alignment starch-binding domain Correspondence S. Janecek Institute of Molecular Biology member of the Centre of Excellence for Molecular Medicine Slovak Academy of Sciences Dubravska cesta 21 SK-84551 Bratislava 45 Slovakia Fax 421 25930 7416 Tel 421 25930 7420 E-mail Received 27 May 2005 revised 13 July 2005 accepted 30 August 2005 doi Approximately 10 of amylolytic enzymes are able to bind and degrade raw starch. Usually a distinct domain the starch-binding domain SBD is responsible for this property. These domains have been classified into families of carbohydrate-binding modules CBM . At present there are six SBD families CBM20 CBM21 CBM25 CBM26 CBM34 and CBM41. This work is concentrated on CBM20 and CBM21. The CBM20 module was believed to be located almost exclusively at the C-terminal end of various amylases. The CBM21 module was known as the N-terminally positioned SBD of Rhizopus glucoamylase. Nowadays many nonamylolytic proteins have been recognized as possessing sequence segments that exhibit similarities with the experimentally observed CBM20 and CBM21. These facts have stimulated interest in carrying out a rigorous bioinformatics analysis of the two CBM families. The present analysis showed that the original idea of the CBM20 module being at the C-terminus and the CBM21 module at the N-terminus of a protein should be modified. Although the CBM20 functionally important tryptophans were found to be

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