Identification of a regulatory phosphorylation site in the hinge 1 region of nitrate reductase from spinach (Spinacea oleracea) leaves

Pauline Douglas, Nick Morrice, Carol MacKintosh

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    Purified nitrate reductase (NR) from spinach leaves was phosphorylated in vitro by NR-inactivating kinase on Ser-543 which is located in the hinge 1 region between the molybdenum-cofactor and haem-binding domains, Phosphorylation of Ser-543 allowed NR to be inhibited by the inhibitor, NIP, Degraded NR preparations in which a proportion of the subunits had lost 45 amino acids from the N-terminus during purification could be phosphorylated by NR kinase on Ser-543, but could not subsequently be fully inhibited by NIP, suggesting a role for the N-terminal tail of NR in NIP binding.

    Original languageEnglish
    Pages (from-to)113-117
    Number of pages5
    JournalFEBS Letters
    Issue number2
    Publication statusPublished - 1995

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