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Fatty acid biosynthesis in yeast.

E Schweizer, K Werkmeister, M K Jain

    Molecular and Cellular Biochemistry
    |November 1, 1978
    PubMed
    Summary
    This summary is machine-generated.

    Researchers studied fatty acid biosynthesis in yeast using mutants. They found that multifunctional proteins, rather than individual enzymes, are favored for kinetics and regulation in this complex biological process.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Yeast Genetics

    Background:

    • Fatty acid biosynthesis is a fundamental cellular process.
    • Understanding the enzymes involved is key to cellular fatty acid composition and regulation.
    • Fatty acid synthetase (FAS) and acetyl CoA carboxylase (ACC) are critical enzymes in this pathway.

    Purpose of the Study:

    • Investigate fatty acid biosynthesis mechanisms in yeast.
    • Determine the contribution of FAS and ACC enzymes to cellular fatty acid composition.
    • Elucidate the molecular structure and genetic control of the FAS complex.

    Main Methods:

    • Utilized fatty acid synthetase and acetyl CoA carboxylase mutants in yeast.
    • Employed genetic and biochemical analyses.

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  • Studied enzyme activities within distinct domains of multifunctional proteins.

    • Main Results:

    • Proposed an alpha6beta6 molecular structure for the FAS complex, with alpha and beta being multifunctional proteins.
    • Identified distinct genes (fas 2 and fas 1) for the alpha and beta subunits, with coordinated biosynthesis.
    • Observed extensive mutual interactions among acyl transferase domains, while other domains were largely independent.

    Conclusions:

    • Multifunctional proteins are favored for fatty acid synthetase biosynthesis due to kinetic and regulatory advantages over individual enzyme complexes.
    • The structure and coordinated biosynthesis of FAS subunits suggest evolutionary optimization.
    • This research provides insights into the complex regulation of fatty acid metabolism.