Literature summary for 3.4.23.B11 extracted from

Hartl, M.; Schweimer, K.; Reger, M.; Schwarzinger, S.; Bodem, J.; Roesch, P.; Woehrl, B.
Formation of transient dimers by a retroviral protease (2010), Biochem. J., 427, 197-203.

Search for more literature for 3.4.23.B11

Inhibitors

Inhibitors	Comment	Organism	Structure
cholic acid	inhibitory to both the separate protease domain and to protease-reverse transcriptase. Cholic acid binds in the proposed protease domain dimerization interface and appears to impair formation of the correct dimer	Simian foamy virus
lithocholic acid	-	Simian foamy virus
additional information	HIV-1 inhibitors darunavir, tipranavir, and indinavir, have no effect on foamy virus protease in vitro	Simian foamy virus

Organism

Organism	UniProt	Comment	Textmining
Simian foamy virus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GB1-GFP + H2O	peptide substrate, harboring the simian foamy virus mac reverse transcriptase-viral integrase cleavage site of the Pol polyprotein, ATQGSYVVHCNTTP, between immunoglobulin binding domain B1 of streptococcal protein G, GB1, and green fluorescent protein, GFP	Simian foamy virus	?	-	?

Subunits

Subunits	Comment	Organism
dimer	transient homodimers of the seaprate protease domain are formed under native conditions but are only present as a minor transient species, which is not detectable by traditional methods	Simian foamy virus

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.6	-	separate protease domain, pH 6.4, 20°C, presence of 3 M NaCl	Simian foamy virus	cholic acid
0.75	-	protease-reverse transcriptase, pH 6.4, 20°C, presence of 3 M NaCl	Simian foamy virus	cholic acid
1	-	protease-reverse transcriptase, pH 6.4, 20°C, presence of 3 M NaCl	Simian foamy virus	lithocholic acid

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Release 2023.1 (January 2023)