What question did this study set out to answer?

To determine why multifunctional peroxisomal and bacterial beta-oxidation enzymes degrade trans-omega-6-unsaturated fatty acid intermediates more efficiently than mitochondrial enzymes.

November 1, 1986Journal of Biological ChemistryOpen Access

Channeling of 3-hydroxy-4-trans-decenoyl coenzyme A on the bifunctional beta-oxidation enzyme from rat liver peroxisomes and on the large subunit of the fatty acid oxidation complex from Escherichia coli.

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Authors

SYSong‐Yu YangThe Graduate Center, CUNY DCD CuebasMissouri State University HSHorst SchulzHelmholtz Centre for Environmental Research

Discussion

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Implication

Enzyme kinetic analysis uncovers substrate channeling in rat peroxisomal and bacterial beta-oxidation complexes, explaining efficient degradation of trans-fatty acids.

Key Points

To determine why multifunctional peroxisomal and bacterial beta-oxidation enzymes degrade trans-omega-6-unsaturated fatty acid intermediates more efficiently than mitochondrial enzymes.
Measured NAD+-dependent oxidation rates of 2-trans,4-trans-decadienoyl-CoA across isolated mitochondrial, peroxisomal, and Escherichia coli enzyme systems.
Analyzed coupled steady-state kinetics and compared the catalytic efficiencies (Vmax/Km) of the enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase steps.
Mitochondrial unlinked enzyme systems failed conventional coupled-reaction kinetic theory due to low equilibrium constants and coupling enzyme concentrations exceeding steady-state intermediate levels.
Peroxisomal bifunctional enzyme and the E. coli fatty acid oxidation complex maintained steady-state velocities equal to hydratase activity despite an unfavorable dehydration-to-dehydrogenation ratio.
Direct channeling of the 3-hydroxy-4-trans-decenoyl-CoA intermediate between active sites accounts for the high degradation rates of trans-fatty acids in peroxisomes.

Cite This Study

Yang et al. (1986) studied this question.

synapsesocial.com/papers/6a756ae133d16877c7f57532 https://doi.org/10.1016/s0021-9258(18)66723-7

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November 1, 1986Journal of Biological ChemistryOpen Access

Channeling of 3-hydroxy-4-trans-decenoyl coenzyme A on the bifunctional beta-oxidation enzyme from rat liver peroxisomes and on the large subunit of the fatty acid oxidation complex from Escherichia coli.

View Full Paper

Ask AI

Bookmark

Authors

SYSong‐Yu YangThe Graduate Center, CUNY DCD CuebasMissouri State University HSHorst SchulzHelmholtz Centre for Environmental Research

Discussion

Member takes

Implication

Enzyme kinetic analysis uncovers substrate channeling in rat peroxisomal and bacterial beta-oxidation complexes, explaining efficient degradation of trans-fatty acids.

Key Points

To determine why multifunctional peroxisomal and bacterial beta-oxidation enzymes degrade trans-omega-6-unsaturated fatty acid intermediates more efficiently than mitochondrial enzymes.
Measured NAD+-dependent oxidation rates of 2-trans,4-trans-decadienoyl-CoA across isolated mitochondrial, peroxisomal, and Escherichia coli enzyme systems.
Analyzed coupled steady-state kinetics and compared the catalytic efficiencies (Vmax/Km) of the enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase steps.
Mitochondrial unlinked enzyme systems failed conventional coupled-reaction kinetic theory due to low equilibrium constants and coupling enzyme concentrations exceeding steady-state intermediate levels.
Peroxisomal bifunctional enzyme and the E. coli fatty acid oxidation complex maintained steady-state velocities equal to hydratase activity despite an unfavorable dehydration-to-dehydrogenation ratio.
Direct channeling of the 3-hydroxy-4-trans-decenoyl-CoA intermediate between active sites accounts for the high degradation rates of trans-fatty acids in peroxisomes.

Cite This Study

Yang et al. (1986) studied this question.

synapsesocial.com/papers/6a756ae133d16877c7f57532 https://doi.org/10.1016/s0021-9258(18)66723-7

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