Mutagenesis of the Dimer Interface Region of Corynebacterium callunae Starch Phosphorylase Perturbs the Phosphate-Dependent Conformational Relay that Enhances Oligomeric Stability of the Enzyme
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,General Medicine
Link
http://academic.oup.com/jb/article-pdf/134/4/599/2511935/mvg178.pdf
Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
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. Starch phosphorylase: Role in starch metabolism and biotechnological applications;Critical Reviews in Biotechnology;2009-08-27
4. Molecular investigation of a novel thermostable glucan phosphorylase from Thermoanaerobacter tengcongensis;Enzyme and Microbial Technology;2007-08
5. Relationships between structure, function and stability for pyridoxal 5′-phosphate-dependent starch phosphorylase from Corynebacterium callunae as revealed by reversible cofactor dissociation studies;European Journal of Biochemistry;2004-07-26
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