Purification and properties of 3-cis-2-trans-enoyl-CoA isomerase (dodecenoyl-CoA delta-isomerase) from rat liver mitochondria.
The mitochondrial enzyme 3-cis-2-trans-enoyl-CoA isomerase, responsible for the positional and geometric isomerization of beta,gamma-unsaturated fatty acyl-CoA intermediates arising during beta-oxidation of unsaturated long chain fatty acids, has been isolated from rat liver, purified to homogeneity by a heat step and a combination of gel filtration and ion-exchange chromatographic procedures. The enzyme has a molecular weight of 30,000, as determined by dodecylsulfate polyacrylamide gel electrophoresis. The isomerase has a strong tendency to form a dimer. It elutes from a calibrated Sephadex G-200 column with an apparent Mr = 60000. The basic isoelectric point, pI 9.0-9.2, is due to its high content in basic amino acids. The amino acid composition determined by the ninhydrin and o-phthalaldehyde detection method is presented.
D000214:Acyl Coenzyme A; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005231:Fatty Acids, Unsaturated; D007535:Isomerases / Q000302:isolation & purification*; D008930:Mitochondria, Liver / Q000201:enzymology*; D008970:Molecular Weight; D051381:Rats
D000214:Acyl Coenzyme A; D000596:Amino Acids; D005231:Fatty Acids, Unsaturated; D007535:Isomerases