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J. Biol. Chem., Vol. 269, Issue 4, 2384-2388, 01, 1994
MJ Luo, TE Smeland, K Shoukry and H Schulz
Mitochondrial delta 3,5, delta 2,4-dienoyl-CoA isomerase, which catalyzes
the conversion of 3,5-octadienoyl-CoA to 2,4-octadienoyl-CoA, was purified
from rat liver 370-fold at almost 30% yield by a six-step purification
procedure. The final preparation appeared to be homogeneous as judged by
gel electrophoresis. The molecular weights of the native enzyme and its
subunit(s) were estimated to be 126,000 and 32,000, respectively. The
purification of delta 3,5, delta 2,4-dienoyl- CoA isomerase completes the
characterization of the enzymes functioning in the NADPH-dependent pathway
for the beta-oxidation of unsaturated fatty acids with double bonds
extending from odd-numbered carbon atoms. This novel pathway may not be
operative in peroxisomes because delta 3,5, delta 2,4-dienoyl-CoA isomerase
was only detected in mitochondria. Substrates of this pathway are
2,5-dienoyl-CoAs formed from 5-enoyl- CoAs by acyl-CoA dehydrogenase. Two
sequential isomerization reactions catalyzed by delta 3, delta 2-enoyl-CoAs
isomerase and delta 3,5, delta 2,4-dienoyl-CoA isomerase, respectively,
convert 2,5-dienoyl-CoAs to 2,4-dienoyl-CoAs, which are reduced by
NADPH-dependent 2,4-dienoyl-CoA reductase (EC 1.3.1.34) before reentering
the beta-oxidation spiral.
Delta 3,5, delta 2,4-dienoyl-CoA isomerase from rat liver mitochondria. Purification and characterization of a new enzyme involved in the beta- oxidation of unsaturated fatty acids
Department of Chemistry, City College, City University of New York, New York 10031.
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