Kinetic Studies of AMP-Dependent Phosphorolysis of Amylopectin Catalyzed by Phosphorylase b on a 27 MHz Quartz-Crystal Microbalance
Author:
Affiliation:
1. Contribution from the Department of Biomolecular Engineering, Frontier Collaborative Research Center, Tokyo Institute of Technology and CREST, Japan Science and Technology Corporation (JST), 4259 Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja046583k
Reference30 articles.
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2. Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phospoenolpyruvate:sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs
3. Substrate-cofactor interactions for glycogen phosphorylase b: a binding study in the crystal with heptenitol and heptulose 2-phosphate
4. Channels at the catalytic site of glycogen phosphorylase b: binding and kinetic studies with the .beta.-glycosidase inhibitor D-gluconohydroximo-1,5-lactone N-phenylurethane
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