Arachidonate 5-lipoxygenase of guinea pig peritoneal polymorphonuclear leukocytes. Activation by adenosine 5'-triphosphate.
Arachidonate 5-lipoxygenase was isolated from guinea pig peritoneal polymorphonuclear leukocytes, and partially purified from a high speed supernatant of a homogenate. 5-Hydroperoxy-6,8,11,14-eicosatetraenoic acid was a predominant reaction product. The enzyme reaction required specifically calcium ion (20 microM for half-maximal activity), and other divalent cations such as magnesium and cobalt were ineffective. The calcium-dependent 5-lipoxygenase reaction was stimulated by several nucleotides, most prominently by ATP in the order of 1 mM. 5,8,11,14,17-Eicosapentaenoic acid as substrate was as active as arachidonic acid, and was oxygenated at the C-5 position.
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D001091:Arachidonate Lipoxygenases; D001202:Ascitic Fluid / Q000166:cytology; D002118:Calcium / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D004789:Enzyme Activation; D006168:Guinea Pigs; D008084:Lipoxygenase / Q000097:blood*; D009504:Neutrophils / Q000187:drug effects / Q000201:enzymology*; D013379:Substrate Specificity
D000255:Adenosine Triphosphate; D001091:Arachidonate Lipoxygenases; D008084:Lipoxygenase; D002118:Calcium