[Adenyl cyclase and adenosine-3',5'-monophosphate phosphodiesteraze: their nature, properties and regulation].
Modern data on the nature, properties and pathways of regulation enzymes, participated metabolism of cyclic, adenosine-3',5'-monophosphate, are described. Much consideration is being given to the problem of regulation of the phosphodiesterase activity due to the effect of Ca2+-binding proteins.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000037:antagonists & inhibitors / Q000378:metabolism / Q000494:pharmacology*; D000067956:Adenylyl Cyclase Inhibitors; D000262:Adenylyl Cyclases / Q000378:metabolism / Q000494:pharmacology*; D000818:Animals; D001951:Brevibacterium / Q000201:enzymology; D002384:Catalysis; D002462:Cell Membrane / Q000201:enzymology; D002477:Cells / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010727:Phosphoric Diester Hydrolases / Q000494:pharmacology*; D011506:Proteins / Q000378:metabolism; D013329:Structure-Activity Relationship
D000067956:Adenylyl Cyclase Inhibitors; D011506:Proteins; D010727:Phosphoric Diester Hydrolases; D015105:3',5'-Cyclic-AMP Phosphodiesterases; D000262:Adenylyl Cyclases
Adeniltsiklaza i fosfodiésteraza adenozin-3',5'-monofosfata: priroda, svoĭstva i reguliatsiia