Literature summary for 3.4.24.15 extracted from

Portaro, F.C.; Hayashi, M.A.; Silva, C.L.; de Camargo, A.C.
Free ATP inhibits thimet oligopeptidase (EC 3.4.24.15) activity, induces autophosphorylation in vitro, and controls oligopeptide degradation in macrophage (2001), Eur. J. Biochem., 268, 887-894.

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Inhibitors

Inhibitors	Comment	Organism	Structure
ADP	-	Rattus norvegicus
ATP	Zn2+ at the active center of the enzyme is the target for the ATP binding to the enzyme leading to the peptidase inhibition and to the enzyme autophosphorylation	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
testis	-	Rattus norvegicus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
o-aminobenzoyl-Gly-Gly-Phe-Leu-Arg-Val-(2,4-dinitrophenyl)ethylenediamine + H2O	-	Rattus norvegicus	?	-	?

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.042	-	ATP	-	Rattus norvegicus
1.25	-	ADP	-	Rattus norvegicus

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Release 2023.1 (January 2023)