Literature summary for 3.4.23.B24 extracted from

Hoshi, M.; Ohki, Y.; Ito, K.; Tomita, T.; Iwatsubo, T.; Ishimaru, Y.; Abe, K.; Asakura, T.
Experimental detection of proteolytic activity in a signal peptide peptidase of Arabidopsis thaliana (2013), BMC Biochem., 14, 16.

Search for more literature for 3.4.23.B24

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Saccharomyces cerevisiae	Arabidopsis thaliana

Inhibitors

Inhibitors	Comment	Organism	Structure
1,3-di-(N-carboxybenzoyl-L-leucyl-L-leucyl) amino acetone	signal peptide peptidase specific inhibitor	Arabidopsis thaliana
[(2R,4R,5S)-2-benzyl-5-(t-butyloxycarbonylamino)-4-hydroxy-6-phenylhexanoyl]-L-leucyl-L-phenylalanine amide	aspartic protease inhibitor that targets signal peptide peptidase or presenilin	Arabidopsis thaliana

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	n-dodecyl-beta-maltoside-solubilized membrane fraction	Arabidopsis thaliana	16020	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
65000	-	x * 65000, SDS-PAGE, fusion construct with green fluorescent protein	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	O81062	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
myc-prolactin-PP-Flag peptide + H2O	human signal peptide peptidase substrate	Arabidopsis thaliana	?	migration of the fragments that are cleaved in SDS-PAGE is identical in size to the fragments produced by human signal peptide peptidase	?

Subunits

Subunits	Comment	Organism
?	x * 65000, SDS-PAGE, fusion construct with green fluorescent protein	Arabidopsis thaliana

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Release 2023.1 (January 2023)