Literature summary for 3.1.3.8 extracted from

Hoiberg-Nielsen, R.; Westh, P.; Arleth, L.
The effect of glycosylation on interparticle interactions and dimensions of native and denatured phytase (2009), Biophys. J., 96, 153-161.

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Organism

Organism	UniProt	Comment	Textmining
Peniophora lycii	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	analysis of second virial coefficients of the heavily glycosylated phytase and its enzymatically deglycosylated counterpart. The native forms of phytase and deglycosylated phytase are equally repulsive at the studied pH 8. When thermally denatured, the second virial coefficient of deglycosylated phytase decreases whereas it remaines unchanged for phytase. The expanding effect of the glycans on the denatured protein conformation relies on steric hindrance that limits the range of torsion angles available to the polypeptide	Peniophora lycii

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	analysis of second virial coefficients of the heavily glycosylated phytase and its enzymatically deglycosylated counterpart. The native forms of phytase and deglycosylated phytase are equally repulsive at the studied pH 8. When thermally denatured, the second virial coefficient of deglycosylated phytase decreases whereas it remaines unchanged for phytase. The expanding effect of the glycans on the denatured protein conformation relies on steric hindrance that limits the range of torsion angles available to the polypeptide	Peniophora lycii

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Release 2023.1 (January 2023)