Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.19.3 extracted from

  • Kaushik, J.K.; Ogasahara, K.; Yutani, K.
    The unusually slow relaxation kinetics of the folding-unfolding of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus (2002), J. Mol. Biol., 316, 991-1003.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C142S/C188S small thermodynamic stability of the mutant enzyme C142S/C188S at low pH. The mutant enzyme is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5. The heat-denaturation of the mutant enzyme is completely reversible at pH 2.3, although the unfolding-refolding reactions are characterized by extremely slow kinetics Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
the heat-denaturation of the mutant enzyme C142S/C188S is completely reversible at pH 2.3, although the unfolding-refolding reactions are characterized by extremely slow kinetics Pyrococcus furiosus

Subunits

Subunits Comment Organism
dimer the mutant enzyme C142S/C188S is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5 Pyrococcus furiosus
monomer the mutant enzyme C142S/C188S is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5 Pyrococcus furiosus
tetramer the mutant enzyme C142S/C188S is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5 Pyrococcus furiosus

Synonyms

Synonyms Comment Organism
pyrrolidone carboxyl peptidase
-
Pyrococcus furiosus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
47
-
thermodynamics of heat denaturation of the monomeric enzyme form of mutant enzyme C142S/C188S at pH 2.3. The mechanism of refolding is a two-state process. The equilibrium establishes with a relaxation time of 5080 s at Tm = 46.5°C Pyrococcus furiosus