Literature summary for 3.4.16.5 extracted from

Dumoulin, M.; Ueno, H.; Hayashi, R.; Balny, C.
Contribution of the carbohydrate moiety to conformational stability of the carboxypeptidase Y high pressure study (1999), Eur. J. Biochem., 262, 475-483.

General Stability

General Stability	Organism
pressure-induced denaturation is a process involving at least three transitions. Low pressure, below 150 mPa, induces slight conformational changes characterized by a slight decrease in the center of the spectral mass of intrinsic fluorescence, whereas no changes in 8-anilino-1-naphthalene sulfonic acid binding fluorescence are observed and 80% of the catalytic activity remains. Higher pressure, 150-500 mPa, induce further conformatiinal changes, characterized by a large decrease in the center of the spectral mass of intrinsic fluorescence, a large increase in the 8-anilino-1-naphthalene sulfonic acid binding fluorescence and the loss of all catalytic activity. A further increase in pressure, above 550 mPa induces transition from this first molten globule-like state to a second malten globule-like state. A similar three-transition process is found for unglycosylated carboxypeptidase Y, but the first two transitions clearly occur at lower pressures than those for glycosylated carboxypeptidase Y	Saccharomyces cerevisiae

Organism

pressure-induced denaturation is a process involving at least three transitions. Low pressure, below 150 mPa, induces slight conformational changes characterized by a slight decrease in the center of the spectral mass of intrinsic fluorescence, whereas no changes in 8-anilino-1-naphthalene sulfonic acid binding fluorescence are observed and 80% of the catalytic activity remains. Higher pressure, 150-500 mPa, induce further conformatiinal changes, characterized by a large decrease in the center of the spectral mass of intrinsic fluorescence, a large increase in the 8-anilino-1-naphthalene sulfonic acid binding fluorescence and the loss of all catalytic activity. A further increase in pressure, above 550 mPa induces transition from this first molten globule-like state to a second malten globule-like state. A similar three-transition process is found for unglycosylated carboxypeptidase Y, but the first two transitions clearly occur at lower pressures than those for glycosylated carboxypeptidase Y

Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	the carbohydrate moiety has a slightly protective role in heat-induced unfolding and highly protective role the enzyme against pressure induced denaturation	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)