Library Faculty/Staff Scholarship and Research
Permanent URI for this collectionhttp://hdl.handle.net/1903/11
Browse
2 results
Search Results
Item Arachidonic acid formed by peroxisomal β-oxidation of 7,10,13,16- docosatetraenoic acid is esterified into 1-acyl-sn-glycero-3-phosphocholine by microsomes(American Society for Biochemistry and Molecular Biology, Inc., 1994) Baykousheva, S. P.; Luthria, D. L.; Sprecher, H.Peroxisomal beta-oxidation of linoleic acid and arachidonic acid was depressed when 1-palmitoyl-sn-glycero-3-phosphocholine and microsomes were included in incubations. This reduction was due to the esterification of the substrate into the acceptor by microsomal 1-acyl-sn-glycero-3- phosphocholine acyltransferase. The first cycle of the beta-oxidation of 7,10,13,16-docosatetraenoic acid was independent of 1-acyl-sn-glycero-3-phosphocholine and microsomes. However, when arachidonate was produced it was esterified rather than serving as a substrate for continued beta-oxidation. When arachidonate and linoleate were incubated with peroxisomes alone, 2-trans-4,7,10-hexadecatetraenoic acid and 2-trans-4-decadienoic acid were the respective end products of beta-oxidation. 2-Oxo-8,11-heptadecadienone, a catabolite produced from linoleate, was most likely a nonenzymatic decarboxylation product of 3-oxo-9,12-octadecadienoic acid. In addition to the termination of beta-oxidation by microsomal-peroxisomal communication, our results with linoleate and arachidonate suggest that the reaction catalyzed by 2-trans-4-cis-dienoyl-CoA reductase is the control step in double bond removal. In addition, the beta-ketothiolase step may play a regulatory role in the peroxisomal beta-oxidation of linoleate but not arachidonate or 7,10,13,16-docosatetraenoic acid.Item Double bond removal from odd-numbered carbons during peroxisomal β- oxidation of arachidonic acid requires both 2,4-dienoyl-CoA reductase and Δ3,5,Δ2,4-dienoyl-CoA isomerase(American Society for Biochemistry and Molecular Biology, Inc., 1995) Luthria, D. L.; Baykousheva, S. P.; Sprecher, H.