Literature summary for 3.4.21.89 extracted from

Bockstael, K.; Geukens, N.; Rao, C.V.; Herdewijn, P.; Anne, J.; Van Aerschot, A.
An easy and fast method for the evaluation of Staphylococcus epidermidis type I signal peptidase inhibitors (2009), J. Microbiol. Methods, 78, 231-237.

Search for more literature for 3.4.21.89

Application

Application	Comment	Organism
analysis	development of a fluorescence resonance energy transfer-based assay method as a rapid and reliable tool in future research for the identification and validation of potential SPase I inhibitors	Staphylococcus epidermidis
drug development	SPase I serves as a potentially interesting target for the development of antibacterials with another mode of action	Staphylococcus epidermidis

Cloned(Commentary)

Cloned (Comment)	Organism
SPase I isozymes, expression of His-tagged Sip2 and Sip3 in Escherichia coli strain BL21(DE3), subcloning in strain TG1	Staphylococcus epidermidis

Inhibitors

Inhibitors	Comment	Organism	Structure
arylomycin A2	a lipohexapeptide SPase I inhibitor, complete inhibition of each of the isozymes at 0.0002 mM by 0.00625 mM inhibitor	Staphylococcus epidermidis
additional information	inhibition by a synthetic substrate-based peptide aldehyde with IC50 of 0.009 mM and 0.013 mM for Sip2 and Sip3, respectively	Staphylococcus epidermidis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
pre-SceD protein + H2O	Staphylococcus epidermidis	substrate of Sip2 and Sip3	SceD + presequence of pre-SceD	-	?

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus epidermidis	-	isozymes Sip1, Sip2, and Sip3, strain 1457	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged Sip2 and Sip3 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Staphylococcus epidermidis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	isozyme Sip1 lacks the catalytic lysine. Development of fluorogenic peptide substrates, protease substrates containing a fluorescent donor chromophore and a quenching acceptor chromophore on either side of the enzyme cleavage site, whose fluorescence is quenched by intramolecular resonance energy transfer, FRET, between donor and a cceptor until the substrate is cleaved by the enzyme allowing continuous measurements, method development and evaluation, overview	Staphylococcus epidermidis	?	-	?
pre-SceD protein + H2O	substrate of Sip2 and Sip3	Staphylococcus epidermidis	SceD + presequence of pre-SceD	-	?

Synonyms

Synonyms	Comment	Organism
Sip1	-	Staphylococcus epidermidis
Sip2	-	Staphylococcus epidermidis
Sip3	-	Staphylococcus epidermidis
Spase I	-	Staphylococcus epidermidis
type I signal peptidase	-	Staphylococcus epidermidis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Staphylococcus epidermidis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Staphylococcus epidermidis

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.0004	-	pH 8.0, 37°C, recombinant isozyme Sip2	Staphylococcus epidermidis	arylomycin A2
0.0008	-	pH 8.0, 37°C, recombinant isozyme Sip3	Staphylococcus epidermidis	arylomycin A2

General Information

General Information	Comment	Organism
physiological function	bacterial SPases I play a key role in protein secretion as they are responsible for the cleavage of signal peptides from secreted proteins	Staphylococcus epidermidis

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Release 2023.1 (January 2023)