Abstract
Anandamide, an endogenous ligand for cannabinoid receptors CB1 and CB2, was incubated with purified Ei-lipoxygenases from barley and tomato. This yielded 11S-hydroperoxy-5,8,12,14-eicosatetraenoylethanolamide (11S-HPANA) as major product (about 70%), This is in contrast with the dioxygenation of arachidonic acid, where 5S-HPETE is the major product. This observation implies that the regiospecificity of the dioxygenation, catalyzed by nonmammalian B-lipoxygenases, is altered by a modification at the carboxylic end of the substrate. Soybean 15-lipoxygenase forms 15S-HPANA (95%) and 11S-HPANA (5%), and in the second dioxygenation 5,15-diHPANA (45%) and 8,15-diHPANA (55%) are formed. Apparently, the regiospecificity of the soybean 15-lipoxygenase reaction is only slightly affected using anandamide as substrate. (C) 1998 Academic Press.
Original language | English |
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Pages (from-to) | 33-38 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 248 |
Issue number | 1 |
Publication status | Published - 9 Jul 1998 |
Keywords
- CANNABINOID RECEPTOR
- SOYBEAN LIPOXYGENASE-1