EC Number   |
General Information |
Reference |
|---|
   3.4.23.41 | malfunction |
an enzyme-deficient mutant displays deregulated pH homeostasis |
754781 |
| 3.4.23.41 | 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 |
-, 733582 |
| 3.4.23.41 | physiological function |
a Candida glabrata mutant lacking all 11 yapsins, possesses an enlarged vacuole and displays phenotypes similar to deficiency in vacuolar membrane ATPase with elevated metal ion susceptibility in an alkaline pH medium and diminished in vacuolar membrane ATPase activity. the mutant shows elevated polyphosphate levels and diminished cellular carboxypeptidase Y activity. A gross perturbation of cellular homoeostasis in the mutant lacking all yapsins, even in the absence of external stressors, is characterized by reduced levels of ATP and stress metabolites, elevated reactive oxygen species levels, cell surface abnormalities, and a constitutively activated protein kinase C signalling pathway. Isoform Yps1 is involved in the maintenance of ion homoeostasis under normal and calcineurin-inhibited conditions |
733295 |
| 3.4.23.41 | physiological function |
complementation analysis of opsA and opsB in kexB mutants: overexpression of opsA or ops B (aspartyl proteases homologous to yeast yapsins YPS1/2) do not suppress the kexB mutation in Aspergillus oryzae or Aspergillus nidulans, although yapsins are multicopy suppressors for the yeast kex2 mutation |
707789 |
| 3.4.23.41 | physiological function |
deletion of the YPS genes generates only minor influence on the sensitivity to cell wall stress |
718457 |
| 3.4.23.41 | physiological function |
deletion of the YPS genes generates only minor influence on the sensitivity to cell wall stress. The sole disruption of YPS1 is sufficient in eliminating the aberrant proteolytic cleavage of recombinant proteins secreted by Hansenula polymorpha |
718457 |
| 3.4.23.41 | physiological function |
disruption of yapsin YPS7 gene confers the mutant cell increased resistance to cell wall perturbing reagents congo red, calcofluor white and sodium dodecyl sulfate. Mutant shows lower content of chitin and increased amounts of beta-1,3-glucan. Disruption of YPS7 gene causes a reduction of the chitin content in lateral cell wall. The inner layer of mutant cell wall, mainly composed of chitin and beta-1, 3-glucan, is much thicker than that in parental strain GS115. The mutant also exhibits increased osmotic resistance compared with the parental strain |
-, 733889 |
| 3.4.23.41 | physiological function |
the enzyme is a potential virulence factor and involved in maturation of proteins and cell wall function |
-, 753595 |
| 3.4.23.41 | physiological function |
the enzyme is required for cell wall maintenance, remodeling and cell-cell interactions. The enzyme is essential for survival in an acidic environment |
754781 |
| 3.4.23.41 | physiological function |
Yps1 is required for cell growth at elevated temperatures |
717611 |
