Catalytic mechanism of scytalone dehydratase from Magnaporthe grisea

D. B. Jordan, G. S. Basarab*, J. J. Steffens, T. Lundqvist, B. R. Pfrogner, R. S. Schwartz, Z. Wawrzak

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    11 Scopus citations


    The catalytic mechanism of scytalone dehydratase was examined by studying alternative substrates and site-directed mutations of active-site residues. Searches for an eno1 intermediate by looking for a half-reaction with authentic scytalone and 3,4-dihydro-6,8-dihydroxy-1-(2H)- 2[13C]naphthalenone were negative. An alternative substrate, 2,3-dihydro- 2,5-dihydroxy-4H-benzopyran-4-one (DDBO), was nearly equal to scytalone as substrate for the enzyme, and DDBO's anomeric effect in stabilizing a partial carbocation center at C3 does not substantially contribute to the mechanism. Kinetic analysis of site-directed mutations of active-site amino acid side chains within the enzyme's active site provided an account for the role of these residues in the enzyme-catalyzed dehydration reactions. A concerted E2 elimination for the catalytic mechanism is proposed.

    Original languageEnglish (US)
    Pages (from-to)277-280
    Number of pages4
    JournalPesticide Science
    Issue number3
    StatePublished - Jan 1 1999


    • Enzyme mechanism
    • Fungal melanin
    • Fungicide
    • Plant disease
    • Scytalone dehydratase
    • X-ray crystallography

    ASJC Scopus subject areas

    • Applied Microbiology and Biotechnology


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