Literature summary extracted from

Eronina, T.B.; Chebotareva, N.A.; Bazhina, S.G.; Makeeva, V.F.; Kleymenov, S.Y.; Kurganov, B.I.
Effect of proline on thermal inactivation, denaturation and aggregation of glycogen phosphorylase b from rabbit skeletal muscle (2009), Biophys. Chem., 141, 66-74.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.4.1.1	proline	concentrations of 0.1 M have a slight accelerating effect on thermal aggregation of glycogen phosphorylase b. The suppression aggregation at high proline concentrations is mainly due to the protective action of proline on the stage of unfolding of the molecule	Oryctolagus cuniculus

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.4.1.1	Oryctolagus cuniculus	-	glycogen phosphorylase b	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
2.4.1.1	skeletal muscle	-	Oryctolagus cuniculus	-

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
2.4.1.1	48	-	half-life about 50 min. In presence of 1.5 M proline, half-life above 150 min. Suppression of thermal aggregation at high proline concentrations is mainly due to the protective action of proline on the stage of unfolding of the molecule	Oryctolagus cuniculus

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Release 2023.1 (January 2023)