Báo cáo khoa học: Tracking interactions that stabilize the dimer structure of starch phosphorylase from Corynebacterium callunae Roles of Arg234 and Arg242 revealed by sequence analysis and site-directed mutagenesis
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Glycogen phosphorylases (GPs) constitute a family ofwidely spread catabolica1,4-glucosyltransferases that areactive as dimers of two identical, pyridoxal 5¢-phosphate-containing subunits. In GP fromCorynebacterium callunae,physiological concentrations of phosphate are requiredto inhibit dissociation of protomers and cause a 100-foldincrease in kinetic stability of the functional quarternarystructure.
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Tracking interactions that stabilize the dimer structure of starch phosphorylase from Corynebacterium callunae Roles of Arg234 and Arg242 revealed by sequence analysis and site-directed mutagenesis
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Tracking interactions that stabilize the dimer structure of starch phosphorylase from Corynebacterium callunae Roles of Arg234 and Arg242 revealed by sequence analysis and site-directed mutagenesis
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