Literature summary for 3.4.21.105 extracted from

Wolf, E.V.; Seybold, M.; Hadravova, R.; Strisovsky, K.; Verhelst, S.H.
Activity-based protein profiling of rhomboid proteases in liposomes (2015), ChemBioChem, 16, 1616-1621 .

Search for more literature for 3.4.21.105

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
(3S,4S)-3-butyl-4-(pent-4-yn-1-yl)oxetan-2-one	-	Escherichia coli
3,4-dichloro-1H-2-benzopyran-1-one	-	Escherichia coli
additional information	inhibitor profiles of rhomboids in micelles and liposomes are similar	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
reconstitution of rhomboids in liposomes. Active rhomboids are reconstituted in large and giant unilamellar vesicles	Escherichia coli

Synonyms

Synonyms	Comment	Organism
GlpG	-	Escherichia coli

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.0056	-	enzyme reconstituted in liposome, pH not specified in the publication, temperature not specified in the publication	Escherichia coli	3,4-dichloro-1H-2-benzopyran-1-one
0.019	-	enzyme reconstituted in micelle, pH not specified in the publication, temperature not specified in the publication	Escherichia coli	3,4-dichloro-1H-2-benzopyran-1-one
0.029	-	enzyme reconstituted in liposome, pH not specified in the publication, temperature not specified in the publication	Escherichia coli	(3S,4S)-3-butyl-4-(pent-4-yn-1-yl)oxetan-2-one
0.044	-	enzyme reconstituted in micelle, pH not specified in the publication, temperature not specified in the publication	Escherichia coli	(3S,4S)-3-butyl-4-(pent-4-yn-1-yl)oxetan-2-one

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Release 2023.1 (January 2023)