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An acyl-thioesterase from yeast mitochondria.

R Stack, S Scharf, J B Ohlrogge

Archives of Biochemistry and Biophysics

|September 1, 1983

Summary

Researchers discovered a novel acyl-coenzyme A thioesterase activity in yeast mitochondria. This enzyme activity, linked to the mitochondrial ATPase complex, prefers oleoyl-coenzyme A as a substrate.

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Area of Science:

Mitochondrial biochemistry
Enzymology
Yeast genetics

Background:

Acyl-coenzyme A thioesterases play roles in fatty acid metabolism.
Mitochondrial function involves complex enzymatic pathways.
Saccharomyces cerevisiae is a model organism for studying cellular processes.

Purpose of the Study:

To characterize a novel acyl-coenzyme A thioesterase activity in yeast mitochondria.
To investigate the relationship between this thioesterase activity and mitochondrial ATPase.
To explore the potential in vivo function of the identified thioesterase.

Main Methods:

Enzyme assays using submitochondrial particles from Saccharomyces cerevisiae.
Substrate specificity testing with oleoyl-coenzyme A.
Inhibition studies with thiol and oxidative phosphorylation inhibitors (oligomycin, venturicidin).
Enzyme purification and characterization, including copurification with mitochondrial ATPase.
Analysis of thioesterase activity in oxidative phosphorylation mutants.

Main Results:

A previously uncharacterized acyl-coenzyme A thioesterase activity was identified in yeast submitochondrial particles.
The enzyme activity preferentially hydrolyzed oleoyl-coenzyme A.
Activity was inhibited by oxidative phosphorylation inhibitors and copurified with mitochondrial ATPase.
Thioesterase activity in resistant mutants also showed resistance to these inhibitors.

Conclusions:

The results strongly suggest that thioester hydrolysis is catalyzed by components associated with the mitochondrial ATPase complex.
The precise in vivo role of this thioesterase activity remains to be elucidated.
Further research is needed to fully understand the function of this enzyme within the mitochondrial system.

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