TAILIEUCHUNG - Báo cáo khoa học: Starch-binding domains in the CBM45 family – low-affinity domains from glucan, water dikinase and a-amylase involved in plastidial starch metabolism

Starch-binding domains are noncatalytic carbohydrate-binding modules that mediate binding to granular starch. The starch-binding domains from the carbohydrate-binding module family 45 (CBM45, ) are found as N-terminal tandem repeats in a small number of enzymes, primarily from photosynthesizing organisms. | IFEBS Journal Starch-binding domains in the CBM45 family - low-affinity domains from glucan water dikinase and a-amylase involved in plastidial starch metabolism Mikkel A. Glaring1 2 Martin J. Baumann1 Maher Abou Hachem1 Hiroyuki Nakai1 Natsuko Nakai1 Diana Santelia3 Bent W. Sigurskjold4 Samuel C. Zeeman3 Andreas Blennow2 and Birte Svensson1 1 Enzyme and Protein Chemistry Department of Systems Biology TechnicalUniversity of Denmark Kongens Lyngby Denmark 2 VKR Research Centre Pro-Active Plants Department of Plant Biology and Biotechnology Faculty of Life Sciences University of Copenhagen Frederiksberg Denmark 3 Department of Biology ETH Zurich Switzerland 4 Department of Biology University of Copenhagen Denmark Keywords carbohydrate-binding module starch metabolism starch-binding domain a-amylase a-glucan water dikinase Correspondence B. Svensson Enzyme and Protein Chemistry Department of Systems Biology TechnicalUniversity of Denmark Soltofts Plads Building 224 DK-2800 Kongens Lyngby Denmark Fax 45 45886307 Tel 45 45252740 E-mail bis@ Received 17 November 2010 revised 5 January 2011 accepted 31 January 2011 doi Starch-binding domains are noncatalytic carbohydrate-binding modules that mediate binding to granular starch. The starch-binding domains from the carbohydrate-binding module family 45 CBM45 http are found as N-terminal tandem repeats in a small number of enzymes primarily from photosynthesizing organisms. Isolated domains from representatives of each of the two classes of enzyme carrying CBM45-type domains the Solanum tuberosum a-glucan water dikinase and the Arabid-opsis thaliana plastidial a-amylase 3 were expressed as recombinant proteins and characterized. Differential scanning calorimetry was used to verify the conformational integrity of an isolated CBM45 domain revealing a surprisingly high thermal stability Tm of C . The functionality of CBM45 was demonstrated in planta by yellow green .

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