Anthranilate synthase of Neurospora crassa: Reaction and labeling with glutamine analogs

James L. Paukert, Jack Henkin, Joseph Keesey, John A. Demoss*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    2 Scopus citations

    Abstract

    The multifunctional enzyme complex, anthranilate synthase from Neurospora crassa, irreversibly loses its glutamine-dependent anthranilate synthase activity on exposure to the reactive glutamine analogs DON and azaserine. Inactivation depends on the presence of the substrate chorismate, is enhanced by the cofactor Mg+2, and is antagonized by glutamine. Inactivation correlates well with the incorporation of [14C]DON into the protein with modification localized to the β subunit (Mr 84,000) of the complex, demonstrating directly that the β subunit provides the glutamine binding site for the glutamine-dependent anthranilate synthase reaction. The slower and less extensive loss of ammonia-dependent anthranilate synthase activity indicates that maximum expression of the ammonia-dependent anthranilate synthase activity by the α subunit also depends on the interaction with an active glutamine amidotransferase domain of the β subunit.

    Original languageEnglish (US)
    Pages (from-to)443-449
    Number of pages7
    JournalArchives of biochemistry and biophysics
    Volume218
    Issue number2
    DOIs
    StatePublished - Oct 15 1982

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology

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