Literature summary for 3.4.23.41 extracted from

Dube, A.K.; Belanger, M.; Gagnon-Arsenault, I.; Bourbonnais, Y.
N-terminal entrance loop of yeast Yps1 and O-glycosylation of substrates are determinant factors controlling the shedding activity of this GPI-anchored endopeptidase (2015), BMC Microbiol., 15, 50.

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Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P32329	-	-
Saccharomyces cerevisiae ATCC 204508	P32329	-	-

Synonyms

Synonyms	Comment	Organism
aspartic proteinase 3	-	Saccharomyces cerevisiae
YPS1	-	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
metabolism	replacement of the N-entrance loop of yapsin Yps1 generates a single chain endopeptidase that undergoes at pH 6.0 partial or at pH 3.0 complete pro-peptide removal. At both pH, the shedding activity of the chimeric endopeptidase, where the N-entrance loop is replaced by the pentapeptide GSVMD found in Yps3, toward Gas1 and itself is strongly and drastically increased, respectively. A direct correlation between endoproteolytic cleavage of this loop in native Yps1 and its shedding is observed. The Yps1-dependent shedding of model glycosylphosphatidylinositol proteins Gas1 and Yps1 is also stimulated by the absence of the O-mannosyltransferases, Pmt4 and Pmt2 respectively. Under these conditions, some Yps1-independent shedding is also observed	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)