The enzymic conversion of 3CIS- and 3Trans-alkenoyl-CoA esters into their 2Trans-isomers

Struijk, C.B.; Beerthuis, R. K.

doi:10.1016/0005-2760(66)90088-9

Cited by 29 publications

(4 citation statements)

References 27 publications

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“…We have also tested rat heart extract, but only a minimum activity of a long-chain isomerase was observed, suggesting a tissue-specific distribution for this isoenzyme in the rat. Struijk & Beerthuis (1966) demonstrated an isomerase of Mr 200000 in bovine liver. In contrast with the enzyme described in this paper, this isomerase showed a preference for short-chain substrates.…”

Section: Discussionmentioning

confidence: 97%

Occurrence of a long-chain Δ3,Δ2-enoyl-CoA isomerase in rat liver

Kilponen

Palosaari

Hiltunen

1990

Biochemical Journal

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Isoproteins of delta 3,delta 2-enoyl-CoA isomerase (EC 5.3.3.8), an auxiliary enzyme in the beta-oxidation of unsaturated fatty acids having double bonds at odd-numbered positions, were studied in livers of control and clofibrate-treated rats. When liver extracts were applied to a hydroxyapatite column at pH 7.0, the previously characterized peroxisomal trifunctional hydratase-dehydrogenase-isomerase enzyme and the mitochondrial isomerase, which shows a preference for short-chain substrates, were eluted almost in parallel. In addition to these activities, a separate isomerase was observed to elute at a lower potassium phosphate concentration in the gradient. Experiments with extracts of purified mitochondria and peroxisomes demonstrated the mitochondrial origin of this third activity. Studies on the kinetic properties of the third isomerase showed that it has a preference for C10-C12 substrates. An Mr of 200,000 was obtained for the native protein by gel-filtration chromatography. Antibodies to mitochondrial short-chain isomerase and peroxisomal trifunctional enzyme did not recognize this novel mitochondrial isoenzyme. The immunological non-cross-reactivity can be interpreted as suggesting that the different isomerases are not closely related at the level of the primary structure of the polypeptide chain. The present data demonstrate that, similar to many other enzymes of beta-oxidation, delta 3,delta 2-enoyl-CoA isomerase has at least three isoenzymes in rat liver: mitochondrial short- and long-chain isomerases and an additional peroxisomal isoenzyme, which in this case is a part of a multifunctional protein.

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Section: Discussionmentioning

confidence: 97%

Occurrence of a long-chain Δ3,Δ2-enoyl-CoA isomerase in rat liver

Kilponen

Palosaari

Hiltunen

1990

Biochemical Journal

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“…(The Km values for all of the substrates listed below are not strikingly different from one another. 245) The data in Table II are even more perplexing in light of the uncertain metabolic role of 3-methyl-3-butenoyl-CoA. An interesting alternative explanation is that the isomerase activity of the ox liver enzyme is an artifact.…”

Section: E Aconitate Isomerasementioning

confidence: 99%

Enzyme-catalyzed allylic rearrangements

Schwab¹,

Henderson²

1990

Chem. Rev.

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“…Enzymes-A search of the data bases for novel genes that contained in their promoters sequences resembling OREs with the consensus CGGN [15][16][17][18]23) and that ended with nucleotides similar to those coding for a peroxisomal targeting signal type 1 (Ref. 41) revealed a homologous pair of open reading frames YLR284c (Fig.…”

Section: Identification Of a Novel S Cerevisiae Open Reading Frame Ementioning

confidence: 99%

“…Human peroxisomal MFE type I and one of the two human mitochondrial isoforms have also been characterized (11)(12)(13). Other ⌬ 3 -cis-⌬ 2 -trans-enoyl-CoA isomerases that have been isolated include those from bovine and porcine mitochondria (14,15) as well as two contained in the glyoxysomes of cucumber seedlings (16,17). The isomerases whose amino acid sequences have been determined belong to the low homology hydratase/isomerase protein family that currently includes over 30 known members (18).…”

mentioning

confidence: 99%

Peroxisomal Δ3-cis-Δ2-trans-Enoyl-CoA Isomerase Encoded by ECI1 Is Required for Growth of the Yeast Saccharomyces cerevisiae on Unsaturated Fatty Acids

Gurvitz

Mursula

Firzinger

et al. 1998

Journal of Biological Chemistry

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We have identified the Saccharomyces cerevisiae gene ECI1 encoding ⌬ 3 -cis-⌬ 2 -trans-enoyl-CoA isomerase that acts as an auxiliary enzyme in the ␤-oxidation of (poly)-unsaturated fatty acids. A mutant devoid of Eci1p was unable to grow on media containing unsaturated fatty acids such as oleic acid but was proficient for growth when a saturated fatty acid such as palmitic acid was the sole carbon source. Levels of ECI1 transcript were elevated in cells grown on oleic acid medium due to the presence in the ECI1 promoter of an oleate response element that bound the transcription factors Pip2p and Oaf1p. Eci1p was heterologously expressed in Escherichia coli and purified to homogeneity. It was found to be a hexameric protein with a subunit of molecular mass 32,000 Da that converted 3-hexenoyl-CoA to trans-2-hexenoyl-CoA. Eci1p is the only known member of the hydratase/isomerase protein family with isomerase and/or 2-enoyl-CoA hydratase 1 activities that does not contain a conserved glutamate at its active site. Using a green fluorescent protein fusion, Eci1p was shown to be located in peroxisomes of wild-type yeast cells. Rat peroxisomal multifunctional enzyme type I containing ⌬ 3 -cis-⌬ 2 -trans-enoyl-CoA isomerase activity was expressed in ECI1-deleted yeast cells, and this restored growth on oleic acid.In mammals, degradation of fatty acids via ␤-oxidation occurs in both peroxisomes and mitochondria; however, in yeast this is solely a peroxisomal process (1). The yeast Saccharomyces cerevisiae is capable of degrading saturated fatty acids in a multistep process catalyzed by the enzymes acyl-CoA oxidase (Pox1p), 2-enoyl-CoA hydratase 2 and D-specific 3-hydroxyacylCoA dehydrogenase (Fox2p), and 3-ketoacyl-CoA thiolase (Pot1p/Fox3p) as shown in Fig. 1 (Refs. 2-5).The only double bonds of unsaturated intermediates that are catabolized via the classical ␤-oxidation pathway are at the ⌬ 2 -position and in the trans-configuration. Therefore, the removal of other double bonds requires the participation of auxiliary enzymes. Fatty acids with double bonds at odd-numbered positions such as oleic acid (cis-C 18:1(9) ) require for their degradation (along with the regular ␤-oxidation enzymes) ⌬ 3

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The enzymic conversion of 3CIS- and 3Trans-alkenoyl-CoA esters into their 2Trans-isomers

Cited by 29 publications

References 27 publications

Occurrence of a long-chain Δ3,Δ2-enoyl-CoA isomerase in rat liver

Occurrence of a long-chain Δ3,Δ2-enoyl-CoA isomerase in rat liver

Enzyme-catalyzed allylic rearrangements

Peroxisomal Δ3-cis-Δ2-trans-Enoyl-CoA Isomerase Encoded by ECI1 Is Required for Growth of the Yeast Saccharomyces cerevisiae on Unsaturated Fatty Acids

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