Effect of protons on the potassium(1+) ion activation of adenosine-5'-monophosphate aminohydrolase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00641a013
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1. Characterization of the metallocenter of rabbit skeletal muscle AMP deaminase. A new model for substrate interactions at a dinuclear cocatalytic Zn site;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2007-12
2. Synthesis of Quaternary Amino Acids Bearing a (2‘Z)-Fluorovinyl α-Branch: Potential PLP Enzyme Inactivators;Organic Letters;2004-05-01
3. Regulation of skeletal muscle AMP deaminase: lysine residues are critical for the pH-dependent positive homotropic cooperativity behaviour of the rabbit enzyme;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;2001-01
4. AMP deaminase from equine muscle: Purification and determination of regulatory properties;International Journal of Biochemistry;1991-01
5. pH-dependent cold libility of rabbit skeletal muscle AMP deaminase;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1983-02
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