Journal of Protein Chemistry

, Volume 12, Issue 1, pp 15–22 | Cite as

PectinaseAspergillus sp. polygalacturonase: Multiplicity, divergence, and structural patterns linking fungal, bacterial, and plant polygalacturonases

  • Eva Stratilová
  • Oskar Markovič
  • Dagmar Škrovinová
  • Lubomíra Rexová-Benková
  • Hans Jörnvall
Article

Abstract

Nine forms ofAspergillus sp. polygalacturonase were purified from a commercial preparation of pectinase Rohament P using chromatographies and chromatofocusing. Individual forms differ in isoelectric point, and at least five differ in structure; whereas molecular masses and enzymatic properties are largely identical. Four forms with freea-amino groups have identical start positions but internal amino acid replacements. Therefore, the multiplicity is derived from true heterogeneities and not from N-terminal truncations. Peptide analysis of the major polygalacturonase reveals large variations toward the enzyme from otherAspergillus species (72–75% residue differences, depending on species) but additional similarities with the enzyme from bacterial and plant sources (only 66–71% residue differences toward theErwinia, tomato, and peach enzymes). Combined with previous data, these facts show polygalacturonase to exhibit extensive multiplicity and much variability, but also unexpected similarities between distantly related forms with conserved functional properties

Key words

Polygalacturonase enzyme multiplicity homology variability conservation 

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Copyright information

© Plenum Publishing Corporation 1993

Authors and Affiliations

  • Eva Stratilová
    • 1
    • 2
  • Oskar Markovič
    • 1
  • Dagmar Škrovinová
    • 1
  • Lubomíra Rexová-Benková
    • 1
  • Hans Jörnvall
    • 2
  1. 1.Institute of ChemistrySlovak Academy of SciencesBratislavaCzechoslovakia
  2. 2.Department of Chemistry IKarolinska InstitutetStockholmSweden

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