pgaD encodes a new type of endopolygalacturonase from Aspergillus niger

L. Parenicova, H.C.M. Kester, J.A.E. Benen, J. Visser

    Research output: Contribution to journalArticleAcademicpeer-review

    48 Citations (Scopus)


    We isolated and characterized a new type of endopolygalacturonase (PG)-encoding gene, pgaD, from Aspergillus niger. The primary structure of PGD differs from that of other A. niger PGs by a 136 amino acid residues long N-terminal extension. Biochemical analysis demonstrated extreme processive behavior of the enzyme on oligomers longer than five galacturonate units. Furthermore, PGD is the only A. niger PG capable of hydrolyzing di-galacturonate. It is tentatively concluded that the enzyme is composed of four subsites. The physiological role of PGD is discussed.
    Original languageEnglish
    Pages (from-to)333-336
    JournalFEBS Letters
    Publication statusPublished - 2000


    • Aspergillus niger
    • Endopolygalacturonase
    • Methylated oligogalacturonate
    • Processivity


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