The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex

P.A Jekel, J.B.H Hartmann, J.J Beintema*

*Corresponding author for this work

    Research output: Contribution to journalArticleAcademicpeer-review

    125 Citations (Scopus)

    Abstract

    The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex, has been determined predominantly with conventional non-automatic methods. The positions of three disulfide bridges have been determined. The sequence has about 60% identity with that of a chitinase from cucumber and 95% with the N-terminal sequence of the lysozyme/chitinase of Parthenocissus quinquefolia. The half-cystine residues in hevein and cucumber chitinase are located at identical positions. Hevamine is a basic protein from the lutoids (vacuoles) of rubber latex and may have a role in plugging the latex vessels and cessation of latex flow. The differences in cellular location, charge properties and sequence between hevamine and cucumber chitinase are similar to those between class I and class II chitinases from tobacco and other plant species.

    Original languageEnglish
    Pages (from-to)123-130
    Number of pages8
    JournalEuropean Journal of Biochemistry
    Volume200
    Issue number1
    DOIs
    Publication statusPublished - 15-Aug-1991

    Keywords

    • AMINO-ACID-SEQUENCE
    • PANULIRUS-INTERRUPTUS HEMOCYANIN
    • SUBUNIT-A
    • PURIFICATION
    • EXPRESSION
    • TOBACCO
    • ACCUMULATION
    • PEPTIDES
    • PROTEINS
    • INVITRO

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