Literature summary for 3.4.19.3 extracted from

Iimura, S.; Umezaki, T.; Takeuchi, M.; Mizuguchi, M.; Yagi, H.; Ogasahara, K.; Akutsu, H.; Noda, Y.; Segawa, S.; Yutani, K.
Characterization of the denatured structure of pyrrolidone carboxyl peptidase from a hyperthermophile under nondenaturing conditions: role of the C-terminal alpha-helix of the protein in folding and stability (2007), Biochemistry, 46, 3664-3672.

Search for more literature for 3.4.19.3

Application

Application	Comment	Organism
additional information	C-terminal alpha-helix in the D1 state plays an important role in retaining the D1 state under the stable conditions and in correctly folding into the native structure of PCP-0SH	Pyrococcus furiosus

Cloned(Commentary)

Cloned (Comment)	Organism
PCP-0SH and its mutant expressed in Escherichia coli strain JM109	Pyrococcus furiosus

Protein Variants

Protein Variants	Comment	Organism
A199P	alpha6-helix region of A199P in the D1 state (initial denatured state) is partially unprotected, while some hydrophobic residues are protected against H/D exchange, although these hydrophobic residues are unprotected in the wild-type protein. Structure of A199P in the D1 state forms a temporary stable denatured structure with a non-native hydrophobic cluster and the unstructured alpha6-helix	Pyrococcus furiosus

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus furiosus	O73944	-	-

Synonyms

Synonyms	Comment	Organism
cysteine-free PCP	-	Pyrococcus furiosus
PCP-0SH	-	Pyrococcus furiosus
pyrrolidone carboxyl peptidase	-	Pyrococcus furiosus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	alpha6-helix (from Ser188 to Glu205) of PCP-0SH is stably formed in the D1 state	Pyrococcus furiosus

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Release 2023.1 (January 2023)