Fungal polygalacturonases exhibit different substrate degradation patterns and differ in their susceptibilities to polygalacturonase-inhibiting proteins
| Autor: | Alan G. Darvill, Peter Albersheim, R. P. Clay, B. J. Cook, Carl Bergmann |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
musculoskeletal diseases
Physiology Molecular Sequence Data Oligosaccharides Cleavage (embryo) Polysaccharide Substrate Specificity Hydrolysis Amino Acid Sequence Pectinase Enzyme Inhibitors Plant Proteins chemistry.chemical_classification biology Sequence Homology Amino Acid Aspergillus niger Fungi Substrate (chemistry) General Medicine biology.organism_classification Chromatography Ion Exchange carbohydrates (lipids) Enzyme Polygalacturonase Biochemistry chemistry Enzyme inhibitor biology.protein Pectins lipids (amino acids peptides and proteins) Agronomy and Crop Science |
| Zdroj: | Molecular plant-microbe interactions : MPMI. 12(8) |
| ISSN: | 0894-0282 |
| Popis: | Polygalacturonic acid (PGA) was hydrolyzed by polygalacturonases (PGs) purified from six fungi. The oligogalacturonide products were analyzed by HPAEC-PAD (high performance anion exchange chromatography-pulsed amperimetric detection) to assess their relative amounts and degrees of polymerization. The abilities of the fungal PGs to reduce the viscosity of a solution of PGA were also determined. The potential abilities of four polygalacturonase-inhibiting proteins (PGIPs) from three plant species to inhibit or to modify the hydrolytic activity of the fungal PGs were determined by colorimetric and HPAEC-PAD analyses, respectively. Normalized activities of the different PGs acting upon the same substrate resulted in one of two distinct oligogalacturonide profiles. Viscometric analysis of the effect of PGs on the same substrate also supports two distinct patterns of cleavage. A wide range of susceptibility of the various PGs to inhibition by PGIPs was observed. The four PGs that were inhibited by all PGIPs tested exhibited an endo/exo mode of substrate cleavage, while the three PGs that were resistant to inhibition by one or more of the PGIPs proceed by a classic endo pattern of cleavage. |
| Databáze: | OpenAIRE |
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