1887

Abstract

produces several extracellular proteases which are believed to be involved in the regulation of the ligninolytic activities of this fungus. Recently, purification and characterization of the most abundant extracellular protease (Sl) have been reported. The sequence of the gene and of the corresponding cDNA has been determined, allowing the identification of its pre- and pro-sequences. A mature protein sequence has been verified by mass spectrometry mapping, the -glycosylation sites have been identified and the glycosidic moieties characterized. Mature Sl shows a cleaved peptide bond in the C-terminal region, which remains associated with the catalytic domain in a non-covalent complex. Reported results indicate that this enzyme is involved in the activation of other secreted proteases, thus suggesting its leading role in cascade activation mechanisms. Analyses of the Sl sequence by homology search resulted in the identification of a DNA sequence encoding a new protease, homologous to Sl, in the genome. A new subgroup of subtilisin-like proteases, belonging to the pyrolysin family, has been defined, which includes proteases from ascomycete and basidiomycete fungi.

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2005-02-01
2019-11-14
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