Tracking interactions that stabilize the dimer structure of starch phosphorylase from Corynebacterium callunae
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1432-1033.2003.03562.x/fullpdf
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4. Glycogen phosphorylase: control by phosphorylation and allosteric effectors;Johnson;FASEB J.,1992
5. Parallel evolution in two homologues of phosphorylase;Rath;Nat. Struct. Biol.,1994
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1. The α-Glucan Phosphorylase MalP of Corynebacterium glutamicum Is Subject to Transcriptional Regulation and Competitive Inhibition by ADP-Glucose;Journal of Bacteriology;2015-04-15
2. 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
3. Stabilization of multimeric enzymes: Strategies to prevent subunit dissociation;Enzyme and Microbial Technology;2009-12
4. Glucosylglycerol and glucosylglycerate as enzyme stabilizers;Biotechnology Journal;2009-11-27
5. “Short-chain” α-1,4-glucan phosphorylase having a truncated N-terminal domain: Functional expression and characterization of the enzyme from Sulfolobus solfataricus;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2009-11
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