Literature summary extracted from

Coffinier, C.; Hudson, S.E.; Farber, E.A.; Chang, S.Y.; Hrycyna, C.A.; Young, S.G.; Fong, L.G.
HIV protease inhibitors block the zinc metalloproteinase ZMPSTE24 and lead to an accumulation of prelamin A in cells (2007), Proc. Natl. Acad. Sci. USA, 104, 13432-13437.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
3.4.24.84	lopinavir	HIV protease inhibitors inhibit ZMPSTE24, leading to an accumulation of farnesyl-prelamin A. The inhibition of ZMPSTE24 by HIV protease inhibitors could play a role in the side effects of these drugs	Mus musculus
3.4.24.84	tipranavir	HIV protease inhibitors inhibit ZMPSTE24, leading to an accumulation of farnesyl-prelamin A. The inhibition of ZMPSTE24 by HIV protease inhibitors could play a role in the side effects of these drugs	Mus musculus

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.4.24.84	Mus musculus	-	recombinantly expressed in yeast	-

Synonyms

EC Number	Synonyms	Comment	Organism
3.4.24.84	Zmpste24	-	Mus musculus

IC50 Value

EC Number	IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
3.4.24.84	0.0012	-	-	Mus musculus	tipranavir
3.4.24.84	0.0184	-	-	Mus musculus	lopinavir

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Release 2023.1 (January 2023)