Purification and characterization of a glucoamylase secreted by the plant pathogen Scierotinia sclerotiorum.
Among the lytic enzymes secreted by the phytopathogen fungus Sclerotinia sclerotiorum, a starch-degrading enzyme has been isolated and characterized. This glycoprotein of 72 kDa is composed of several isoforms ranging from pI 4.8 to 5.4. The enzymatic parameters have been determined. Specificity studies together with the analysis of the reaction products show that it is an alpha-1,4-glucanohydrolase. This result is also corroborated by the analysis of the N-terminal and two inner amino acids sequences that are very similar to fungal glucoamylase genes or enzymes so far sequenced.
Martel
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MB
Laboratoire de biologie cellulaire fongique (UMR 5122) Université Lyon I Villeurbanne, France.
Hervé du Penhoat
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C
Létoublon
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Fèvre
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M
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001203:Ascomycota / Q000201:enzymology* / Q000254:growth & development / Q000472:pathogenicity; D005087:Glucan 1,4-alpha-Glucosidase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D006368:Helianthus / Q000382:microbiology; D008969:Molecular Sequence Data; D010935:Plant Diseases / Q000382:microbiology; D013213:Starch / Q000378:metabolism; D013379:Substrate Specificity
D000596:Amino Acids; D013213:Starch; D005087:Glucan 1,4-alpha-Glucosidase