Publications

• [The metabolism of unsaturated fatty acid. 3. On the beta-oxidation of mono- and polyene-fatty acids. The mechanism of the enzymatic reaction on delta-3-cis-enoyl-CoA compounds].

  Stoffel W., Ditzer R., Caesar H.

  Hoppe Seylers Z Physiol Chem 339:167-181(1964) [PubMed] [EuropePMC]

• Purification of hog liver isomerase. Mechanism of isomerization of 3-alkenyl and 3-alkynyl thioesters.

  Miesowicz F.M., Bloch K.

  A hog liver enzyme that catalyzes the reversible conversion of 3-acetylenic fatty acyl thioester to (+)-2,3-dienoyl fatty acyl thioester has been purified to homogeneity. The enzyme is not inhibited by the allenic product that it generates. The same homogenous enzyme catalyzes the conversions of 3 ... >> More

  A hog liver enzyme that catalyzes the reversible conversion of 3-acetylenic fatty acyl thioester to (+)-2,3-dienoyl fatty acyl thioester has been purified to homogeneity. The enzyme is not inhibited by the allenic product that it generates. The same homogenous enzyme catalyzes the conversions of 3-cis- or 3-trans-acyl Coenzyme A derivatives to 2-trans-acyl-CoA derivatives. Four forms of the isomerase differing in charge (pI = 6.57, 6.83, 7.01, and 7.27) have been separated by isoelectric focusing. Ultracentrifugation and sodium dodecyl sulfate-gel electrophoresis indicate that each of these enzyme forms is dimeric and composed of two 45,000-dalton subunits. With 3-acetylenic substrates, all enzyme forms exhibit broad specificity for chain length (C6 to C12) and for the thioester moiety (N-acetylcysteamine (NAC), pantetheine, or CoA). The 3-cis and 3-trans olefinic substrates are active only in the form of their coenzyme A derivatives; their NAC thioesters inhibit competitively. Mechanistic studies favor an isomerization pathway by way of carbanion intermediates. The acetylene-allene isomerase described here and the reported crotonase-catalyzed hydration of allenic thioesters (Branchini, B.R., Miesowicz, F.M., and Bloch, K. (1977) Bioorg. Chem. 6, 49-52) may be responsible for the degradation of naturally occurring acetylenic and allenic acids. << Less

  J Biol Chem 254:5868-5877(1979) [PubMed] [EuropePMC]

• Functional characterization of delta3,delta2-enoyl-CoA isomerases from rat liver.

  Zhang D., Yu W., Geisbrecht B.V., Gould S.J., Sprecher H., Schulz H.

  The degradation of unsaturated fatty acids by beta-oxidation involves Delta(3),Delta(2)-enoyl-CoA isomerases (enoyl-CoA isomerases) that catalyze 3-cis --> 2-trans and 3-trans --> 2-trans isomerizations of enoyl-CoAs and the 2,5 --> 3,5 isomerization of dienoyl-CoAs. An analysis of rat liver enoyl ... >> More

  The degradation of unsaturated fatty acids by beta-oxidation involves Delta(3),Delta(2)-enoyl-CoA isomerases (enoyl-CoA isomerases) that catalyze 3-cis --> 2-trans and 3-trans --> 2-trans isomerizations of enoyl-CoAs and the 2,5 --> 3,5 isomerization of dienoyl-CoAs. An analysis of rat liver enoyl-CoA isomerases revealed the presence of a monofunctional enoyl-CoA isomerase (ECI) in addition to mitochondrial enoyl-CoA isomerase (MECI) in mitochondria, whereas peroxisomes contain ECI and multifunctional enzyme 1 (MFE1). Thus ECI, which previously had been described as peroxisomal enoyl-CoA isomerase, was found to be present in both peroxisomes and mitochondria. This enzyme seems to be identical with mitochondrial long-chain enoyl-CoA isomerase (Kilponen, J.M., Palosaari, P.M., and Hiltunen, J.K. 1990. Biochem. J. 269, 223-226). All three hepatic enoyl-CoA isomerases have broad chain length specificities but are distinguishable by their preferences for one of the three isomerization reactions. MECI is most active in catalyzing the 3-cis --> 2-trans isomerization; ECI has a preference for the 3-trans --> 2-trans isomerization, and MFE1 is the optimal isomerase for the 2,5 --> 3,5 isomerization. A functional characterization based on substrate specificities and total enoyl-CoA isomerase activities in rat liver leads to the conclusion that the 3-cis --> 2-trans and 2,5 --> 3,5 isomerizations in mitochondria are catalyzed overwhelmingly by MECI, whereas ECI contributes significantly to the 3-trans --> 2-trans isomerization. In peroxisomes, ECI is predicted to be the dominant enzyme for the 3-cis --> 2-trans and 3-trans --> 2-trans isomerizations of long-chain intermediates, whereas MFE1 is the key enzyme in the 2,5 --> 3,5 isomerization. << Less

  J. Biol. Chem. 277:9127-9132(2002) [PubMed] [EuropePMC]

  This publication is cited by 8 other entries.

• Purification and properties of 3-cis-2-trans-enoyl-CoA isomerase (dodecenoyl-CoA delta-isomerase) from rat liver mitochondria.

  Stoffel W., Grol M.

  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 homogenei ... >> More

  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. << Less

  Hoppe Seylers Z Physiol Chem 359:1777-1782(1978) [PubMed] [EuropePMC]