Quantitative structure activity relationship studies on the activation of yeast AMP deaminase by polyamines.
Quantitative structure activity relationship studies on the activation of AMP deaminase by polyamines were carried out. Polyamine enhanced the maximal velocity of AMP deaminase without changing the affinity for the substrate AMP. Activation by polyamines of AMP deaminase can be accounted for by the simple Michaelis-Menten mechanism in the presence of ATP. A close correlation between the structure and activation constants for polyamines suggests that the binding of polyamine to AMP deaminase involves primarily polar interactions.
D000659:AMP Deaminase / Q000378:metabolism*; D000249:Adenosine Monophosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D007700:Kinetics; D009709:Nucleotide Deaminases / Q000378:metabolism*; D011073:Polyamines / Q000378:metabolism / Q000494:pharmacology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013329:Structure-Activity Relationship
D011073:Polyamines; D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D009709:Nucleotide Deaminases; D000659:AMP Deaminase