Cerevisin
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.21 Serine endopeptidases > 3.4.21.48 cerevisin
Cerevisin is a yeast subtilisin-like serine endopeptidase in family S8 from Saccharomyces cerevisiae, containing a Cys near active-site His and inhibited by mercurials (proteinase ycaB from Candida albicans is similar); it hydrolyses proteins with broad specificity and Bz-Arg-OEt and Ac-Tyr-OEt, but does not hydrolyse peptide amides. By digesting vacuolar proteins it supports yeast protein turnover. It appears in viruses and cellular organisms.
Cerevisin is a yeast subtilisin-like serine endopeptidase in family S8 from Saccharomyces cerevisiae, containing a Cys near active-site His and inhibited by mercurials (proteinase ycaB from Candida albicans is similar); it hydrolyses proteins with broad specificity and Bz-Arg-OEt and Ac-Tyr-OEt, but does not hydrolyse peptide amides. By digesting vacuolar proteins it supports yeast protein turnover. It appears in viruses and cellular organisms.
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