title: Interaction of rat muscle AMP deaminase with myosin. II. Modification of the kinetic and regulatory properties of rat muscle AMP deaminase by myosin.
abstract: The problems of whether the kinetic and regulatory properties of AMP deaminase were modified by formation of a deaminase-myosin complex were investigated with an enzyme preparation from rat skeletal muscle. Results showed that AMP deaminase was activated by binding to myosin. Myosin-bound AMP deaminase showed a sigmoidal activity curve with respect to AMP concentration in the absence of ATP and ADP, but a hyperbolic curve in their presence. Addition of ATP and ADP doubled the V value, but did not affect the Km value. Myosin-bound AMP deaminase also gave a sigmoidal curve in the presence of alkali metal ions, whereas free AMP deaminase gave a hyperbolic curve. GTP abolished the activating effects of both myosin and ATP.
mesh_terms: D000659:AMP Deaminase / Q000378:metabolism*; D000818:Animals; D003285:Contractile Proteins / Q000494:pharmacology; D004789:Enzyme Activation; D007527:Isoenzymes / Q000378:metabolism; D007700:Kinetics; D008297:Male; D009132:Muscles / Q000201:enzymology / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism / Q000494:pharmacology*; D009709:Nucleotide Deaminases / Q000378:metabolism*; D009928:Organ Specificity; D011485:Protein Binding; D051381:Rats; D012265:Ribonucleotides / Q000494:pharmacology
chemical_list: D003285:Contractile Proteins; D007527:Isoenzymes; D012265:Ribonucleotides; D009709:Nucleotide Deaminases; D000659:AMP Deaminase; D009218:Myosins