Literature summary for 3.4.11.15 extracted from

Rosenbaum, E.; Gabel, F.; Dura, M.A.; Finet, S.; Clery-Barraud, C.; Masson, P.; Franzetti, B.
Effects of hydrostatic pressure on the quaternary structure and enzymatic activity of a large peptidase complex from Pyrococcus horikoshii (2012), Arch. Biochem. Biophys., 517, 104-110.

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Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	the enzymatic activity is enhanced by pressure up to 180 MPa. The enzyme is active under hydrostatic pressure of up to 350 MPa	Pyrococcus horikoshii

General Stability

General Stability	Organism
high robustness of the oligomeric enzyme under high pressure of up to 300 MPa at 25°C as well as at 90°C	Pyrococcus horikoshii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	L-lysine 4-nitroanilide	KM-value as a function of pressure	Pyrococcus horikoshii

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	O59485	-	-
Pyrococcus horikoshii OT-3	O59485	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-lysine 4-nitroanilide + H2O	-	Pyrococcus horikoshii	L-lysine + 4-nitroaniline	-	?
L-lysine 4-nitroanilide + H2O	-	Pyrococcus horikoshii OT-3	L-lysine + 4-nitroaniline	-	?

Synonyms

Synonyms	Comment	Organism
PhTET3	-	Pyrococcus horikoshii
TET3	-	Pyrococcus horikoshii

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Release 2023.1 (January 2023)