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Yeast fatty acid synthase: structure to function relationship.

N Singh, S J Wakil, J K Stoops

|November 5, 1985

Summary

Yeast fatty acid synthase has six active sites for fatty acid synthesis. These sites function independently, as demonstrated by active site titration experiments.

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Area of Science:

Biochemistry
Molecular Biology

Background:

Yeast fatty acid synthase (FAS) is a large, multifunctional enzyme complex.
It exists as an alpha 6 beta 6 complex, with seven catalytic activities divided between subunits.
The organization and operational mode of its six potential fatty acid synthesis centers are debated.

Purpose of the Study:

To investigate the operational mode of the six fatty acid synthesis centers in yeast FAS.
To distinguish between models of functionally independent centers versus half-sites activity.

Main Methods:

Active site titration was performed by quantifying fatty acyl product formation without turnover.
Substrates used were p-nitrophenyl thioacetate and thiophenyl malonate with NADPH, omitting coenzyme A.
Product quantitation involved gas-liquid chromatography and radioactivity measurement using p-nitrophenyl thio [1-14C] acetate.

Main Results:

A stoichiometry of approximately six moles of fatty acid synthesized per mole of alpha 6 beta 6 complex was determined.
This quantitative result was consistent across both chromatographic and radiometric methods.

Conclusions:

The results indicate the presence of six independently functioning centers for fatty acid synthesis within the yeast alpha 6 beta 6 FAS complex.
This supports the model of functionally independent catalytic centers over half-sites activity.

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