Literature summary extracted from

Dee, D.; Pencer, J.; Nieh, M.P.; Krueger, S.; Katsaras, J.; Yada, R.Y.
Comparison of solution structures and stabilities of native, partially unfolded and partially refolded pepsin (2006), Biochemistry, 45, 13982-13992.

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.4.23.1	Sus scrofa	-	-	-

Renatured (Commentary)

EC Number	Renatured (Comment)	Organism
3.4.23.1	acid refolded pepsin has secondary and tertiary structures intermediate between the alkaline denatured and native forms but is thermodynamically stable relative to the native state. The acid refolded state of pepsin is dependent on the protein concentration during refolding. Both the secondary and tertiary structures of concentrated-refolded pepsin are native-like, in contrast to the intermediate nature of acid refolded pepsin, refolded under dilute concentration. Despite a native-like conformation, concentrated-refolded pepsin is more stable and has substantially reduced activity compared to that of the native state, suggesting that the protein is misfolded. It is proposed that the stable but misfolded, acid-refolded states are evidence that pepsin in its native conformation is metastable	Sus scrofa

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.4.23.1	KPAEFF(NO2)-AL + H2O	-	Sus scrofa	?	-	?

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Release 2023.1 (January 2023)