Analysis of myo-inositol hexakisphosphate hydrolysis by Bacillus phytase: Indication of a novel reaction mechanism

J. Kerovuo, J. Rouvinen, Frank-Andreas Hatzack

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    Phytic acid (myo-inositol hexakisphosphate, InsP(6)) hydrolysis by Bacillus phytase (PhyC) was studied. The enzyme hydrolyses only three phosphates from phytic acid. Moreover, the enzyme seems to prefer the hydrolysis of every second phosphate over that of adjacent ones. Furthermore, it is very likely that the enzyme has two alternative pathways for the hydrolysis of phytic acid, resulting in two different myo-inositol trisphosphate end products: Ins(2,4,6)P-8 and Ins(1,3,5)P-3. These results, together with inhibition studies with fluoride, vanadate, substrate and a substrate analogue, indicate a reaction mechanism different from that of other phytases. By combining the data presented in this study with (1) structural information obtained from the crystal structure of Bacillus amyloliquefaciens phytase [Ha, Oh, Shin, Kim, Oh, Kim, Choi and Oh (2000) Nat. Struct. Biol. 7, 147-153], and (2) computer-modelling analyses of enzyme-substrate complexes, a novel mode of phytic acid hydrolysis is proposed.
    Original languageEnglish
    JournalBiochemical Journal
    Volume352
    Pages (from-to)623-628
    ISSN0264-6021
    DOIs
    Publication statusPublished - 2000

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