The specificity of yeast low-Km cyclic AMP phosphodiesterase towards free bivalent metal ions and the diastereoisomers of cyclic adenosine phosphorothioate.
The relative activity of a zinc-containing cyclic AMP phosphodiesterase towards the (Sp)- compared with the (Rp)-diastereoisomer of cyclic adensine phosphorothioate varied with the identity of the free bivalent metal ion from more than 35 to 0.074 along the series Mg2+ greater than Mn2+ greater than Co2+ greater than Zn2+ greater than Cd2+, showing that this ion, and not the tightly bound zinc, bonds to the phosphorothioate moiety of the substrate.
Suoranta
K
K
Londesborough
J
J
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000378:metabolism*; D002413:Cations, Divalent / Q000494:pharmacology*; D000242:Cyclic AMP / Q000031:analogs & derivatives* / Q000494:pharmacology; D006868:Hydrolysis; D007700:Kinetics; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000201:enzymology*; D013237:Stereoisomerism; D013873:Thionucleotides / Q000494:pharmacology*
D002413:Cations, Divalent; D013873:Thionucleotides; C016957:adenosine-3',5'-cyclic phosphorothioate; D000242:Cyclic AMP; D015105:3',5'-Cyclic-AMP Phosphodiesterases