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Literature summary for 3.4.21.26 extracted from

  • Czekster, C.M.; Naismith, J.H.
    Kinetic landscape of a peptide bond-forming prolyl oligopeptidase (2017), Biochemistry, 56, 2086-2095 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Galerina marginata

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.051
-
IWGIGCNPWTAEHVDQTLASGNDIC at pH 8.0 and 37°C Galerina marginata
0.0554
-
IWGIGCNPWTAEHVDQTLASGNDIC at pH 8.0 and 20°C Galerina marginata

Organism

Organism UniProt Comment Textmining
Galerina marginata
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HisTrap column chromatography, HiTrap Q column chromatography, and Superdex S200 gel filtration Galerina marginata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
IWGIGCNPWTAEHVDQTLASGNDIC + H2O a peptide with 25 amino acids (25mer, sequence IWGIGCNPWTAEHVDQTLASGNDIC) is utilized by the enzyme as a substrate for the macrocyclization reaction. During the macrocyclase reaction, the enzyme generates an eight-amino acid cyclic peptide from the N-terminal residues (the core, sequence IWGIGCNP), cleaving off the 17-C-terminal amino acid recognition sequence (peptide tail, sequence WTAEHVDQTLASGNDIC) Galerina marginata cyclic IWGIGCNP + WTAEHVDQTLASGNDIC
-
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Synonyms

Synonyms Comment Organism
POPB
-
Galerina marginata
prolyl oligopeptidase B
-
Galerina marginata

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.23
-
IWGIGCNPWTAEHVDQTLASGNDIC at pH 8.0 and 20°C Galerina marginata
0.58
-
IWGIGCNPWTAEHVDQTLASGNDIC at pH 8.0 and 37°C Galerina marginata