Relationships between structure, function and stability for pyridoxal 5′-phosphate-dependent starch phosphorylase from Corynebacterium callunae as revealed by reversible cofactor dissociation studies
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.2004.04265.x/fullpdf
Reference29 articles.
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2. α-Glucan phosphorylases - chemical and physical basis of catalysis and regulation;Graves;Ann. Rev. Biochem.,1972
3. Complementation of subunits from glycogen phosphorylases of frog and rabbit skeletal muscle and rabbit liver;Feldmann;Eur. J. Biochem.,1976
4. Association-dissociation properties of sodium borohydride-reduced phosphorylase b;Tu;J. Biol. Chem.,1973
5. Interactions between native and chemically modified subunits of matrix-bound glycogen phosphorylase;Feldmann;Proc. Natl Acad. Sci. USA,1972
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5. Orthophosphate binding at the dimer interface of Corynebacterium callunae starch phosphorylase: mutational analysis of its role for activity and stability of the enzyme;BMC Biochemistry;2010
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