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2-aminobenzoyl-LPATG-diaminopropionic acid + H2O
2-aminobenzoyl-LPAT + G-diaminopropionic acid
-
efficient cleavage
-
-
?
2-aminobenzoyl-LPNTA-diaminopropionic acid + H2O
2-aminobenzoyl-LPNT + A-diaminopropionic acid
-
small amount of cleavage
-
-
?
4-([4-(dimethylamino)phenyl]-azo)-benzoyl-QALPETGEE-((2-aminoethyl)-amino)naphthalene-1-sulfonic acid + H2O
?
-
a catalytically important and conserved binding surface is formed by residues A118, T180 and I182. R197 is also required for catalysis
-
-
?
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Gln-Ala-Leu-Pro-Glu-Thr-Gly-Glu-Glu-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid + H2O
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Gln-Ala-Leu-Pro-Glu-Thr + Gly-Glu-Glu-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
-
-
-
-
?
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Leu-Pro-Glu-Thr-Gly-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid + H2O
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Leu-Pro-Glu-Thr + Gly-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
-
-
-
-
?
5(6)-carboxyfluorescein-6-aminohexanoic acid-LPKTGGRR-NH2 + H2O
?
-
-
-
-
?
A33-LPETG-His6 + H2O
?
-
A33 antigen extracellular domain bearing a His6 tag
-
-
?
Abz-KVENPQTNAGT-Dap(Dnp)-NH2 + GGGGG
Abz-KVENPQTGGGGG + Gly-Dap(DNP)-NH2
-
-
-
-
?
Abz-LPETG-Dap(Dnp) + GGGGG
Abz-LPETGGGGG + G-Dap(Dnp)
-
-
-
-
?
Abz-LPETG-Dap(Dnp) + Gly5
?
-
-
-
-
?
Abz-LPETG-Dap(Dnp) + H2O
?
Abz-LPETG-Dap(Dnp) + H2O
Abz-LPET + G-Dap(Dnp)
Abz-LPETG-Dap(Dnp)-NH2 + GGGGG
?
-
-
-
-
?
Abz-LPETG-Dap(Dnp)-NH2 + GGGGG
Abz-LPETGGGGGG + Gly-Dap(Dnp)-NH2
-
-
-
-
?
Abz-LPETG-Dap(Dnp)-NH2 + Gly5
?
-
transpeptidation of LPXTG-containing peptides to the cell-wall precursor mimic NH2-Ala2
-
-
?
Abz-LPETG-Dap(Dnp)-NH2 + Gly5
Abz-LPETGGGGG-OH + Gly-Dap(Dnp)-NH2
-
-
-
-
?
Abz-LPETG-Dap(Dnp)-NH2 + H2O
?
-
-
-
-
?
Abz-LPETGG-Dap(Dnp)-NH2 + Ala-Ala
Abz-LPETAA + GG-Dap(Dnp)-NH2
Abz-LPETGG-Dap(Dnp)-NH2 + GGGGG
Abz-LPETGGGGGG + Gly-Dap(Dnp)-NH2
-
-
-
-
?
Abz-LPKTGK(Dnp)KK + GGGWW
Abz-LPKTGGGWW + GK(Dnp)KK
-
substrate peptide 1 (Abz-LPKTGK(Dnp)KK) and acceptor peptide 2 (GGGWW)
-
-
?
acetyl-ooocctcttacctcagttacaoooLPKTGGR-NH2 + H-GGGKLALKLALKALKAALKLA-NH2
acetyl-ooocctcttacctcagttacaoooLPKTGGGKLALKLALKALKAALKLA-NH2 + H-GGR-NH2
-
-
-
-
?
agmatine + YALPETGK
(NH2)2-CN-(CH2)4-NH-(CO)-TEPLAY + ?
-
transpeptidase reaction. The initially formed acyl-enzyme intermediate undergoes a hydrolysis followed by intra-molecular transpeptidation
-
-
?
AHLPKTGLR + 5-aminopentan-1-ol
?
-
-
-
-
?
AHLPKTGLR + 6-aminohexyl 4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
?
-
-
-
-
?
AHLPKTGLR + N-(2-(2-ethoxyethoxy)ethanamine)biotin amide
?
-
-
-
-
?
AHLPKTGLR + N-hexylbiotin amide
?
-
-
-
-
?
AHLPKTGLR-NH2 + triglycine
?
-
-
-
-
?
aminobenzoyl-LPETG-dinitrophenyl ester + Gly-Gly-Gly
aminobenzoyl-LPETGGG + Gly-dinitrophenyl ester
-
HPLC results provide direct evidence for the formation of the kinetically competent acyl enzyme intermediate
-
-
?
Dabcyl-LPETG-EDANS + H2O
Dabcyl-LPET + Gly-EDANS
-
-
-
-
?
Dabcyl-QALPETGEE-Edans + H2O
Dabcyl-QALPET + GEE-Edans
Dabcyl-SFLPKTGM-EDANS + H2O
?
Dnp-AQALPETGEE-NH2 + Gly5
?
-
-
-
-
?
Dns-LPKTGGRR + GGGWW
Dns-LPKTGGGWW + GGRR
-
dansyl-labeled Dns-LPKTGGRR substrate peptide and acceptor peptide 2 (GGGWW)
-
-
?
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-2,4-dinitrophenyl ester + Gly-Gly-Gly
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-Gly-Gly + Gly-2,4-dinitrophenyl ester
-
ping-pong mechanism in which a common acyl-enzyme intermediate is formed in transpeptidation and hydrolysis. The nucleophile binding site of the enzyme is specific for diglycine. The S1' and S2' sites of the sortase both prefer a glycine residue, the S1' site is exclusively selective for glycine
-
-
?
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-2,4-dinitrophenyl ester + H2O
o-aminobenzoyl-Leu-Pro-Glu-Thr + Gly-2,4-dinitrophenyl ester
-
ping-pong mechanism in which a common acyl-enzyme intermediate is formed in transpeptidation and hydrolysis. The nucleophile binding site of the enzyme is specific for diglycine. The S1' and S2' sites of the sortase both prefer a glycine residue, the S1' site is exclusively selective for glycine
-
-
?
o-aminobenzoyl-LPETG-2,4-dinitrophenyl + H2O
o-aminobenzoyl-LPETG + 2,4-dinitrophenol
-
-
-
-
?
o-aminobenzoyl-LPETG-2,4-dinitrophenyl ester + H2O
?
-
-
-
-
?
recombinant Helicobacter pylori R1,3-fucosyltransferase + triglycine
?
-
-
-
-
?
recombinant human beta1,4-galactosyltransferase + N-(2-(2-ethoxyethoxy)ethanamine)biotin amide
?
-
-
-
-
?
recombinant human beta1,4-galactosyltransferase + N-hexylbiotin amide
?
-
-
-
-
?
YALPETGK + H2O
YALPET + Gly-Lys
-
-
-
-
?
[4-(4-dimethylaminophenylazo)benzoic acid]-QALPETGEE-[5-[2'-(aminoethyl)amino]-naphthalenesulfonic acid] + H2O
?
-
-
-
-
?
additional information
?
-
Abz-LPETG-Dap(Dnp) + H2O
?
-
-
-
-
?
Abz-LPETG-Dap(Dnp) + H2O
?
-
evidence for a reverse protonation catalytic mechanism
-
-
?
Abz-LPETG-Dap(Dnp) + H2O
Abz-LPET + G-Dap(Dnp)
-
cleavage between the threonine and the glycine residues, efficient cleavage
-
-
?
Abz-LPETG-Dap(Dnp) + H2O
Abz-LPET + G-Dap(Dnp)
-
-
-
-
?
Abz-LPETGG-Dap(Dnp)-NH2 + Ala-Ala
Abz-LPETAA + GG-Dap(Dnp)-NH2
transpeptidation of LPXTG-containing peptides to the cell-wall precursor mimic AlaAla
-
-
?
Abz-LPETGG-Dap(Dnp)-NH2 + Ala-Ala
Abz-LPETAA + GG-Dap(Dnp)-NH2
transpeptidation of LPXTG-containing peptides to the cell-wall precursor mimic AlaAla
-
-
?
Dabcyl-QALPETGEE-Edans + H2O
Dabcyl-QALPET + GEE-Edans
-
-
-
-
?
Dabcyl-QALPETGEE-Edans + H2O
Dabcyl-QALPET + GEE-Edans
-
-
-
-
?
Dabcyl-SFLPKTGM-EDANS + H2O
?
-
the substrate mimicks the LPXTG motif of pilus 2a minor ancillary protein
-
-
?
Dabcyl-SFLPKTGM-EDANS + H2O
?
-
the substrate mimicks the LPXTG motif of pilus 2a minor ancillary protein
-
-
?
GST-LPETG + G-eGFP
?
-
G-eGFP = enhanced green fluorescent protein with a glycine at the N-terminus, protein-protein ligation reaction
-
-
?
GST-LPETG + G-eGFP
?
-
G-eGFP = enhanced green fluorescent protein with a glycine at the N-terminus, protein-protein ligation reaction
-
-
?
PrtP protein + H2O
?
-
-
-
-
?
PrtP protein + H2O
?
-
-
-
-
?
YbeF protein + H2O
?
-
-
-
-
?
YbeF protein + H2O
?
-
-
-
-
?
YhgE protein + H2O
?
-
-
-
-
?
YhgE protein + H2O
?
-
-
-
-
?
YndF protein + H2O
?
-
-
-
-
?
YndF protein + H2O
?
-
-
-
-
?
YwfG protein + H2O
?
-
-
-
-
?
YwfG protein + H2O
?
-
-
-
-
?
additional information
?
-
-
sortase A may be critical in the early stage of inhaltation anthrax
-
-
?
additional information
?
-
-
no cleavage of 2-aminobenzoyl-NPKTG-diaminopropionic acid and 2-aminobenzoyl-LGATG-diaminopropionic acid
-
-
?
additional information
?
-
-
SrtA recognizes the LPXTG-sorting signal through a lock-in-key mechanism
-
-
?
additional information
?
-
-
two elements of Spa pilin precursor, the pilin motif and the sorting signal, are together sufficient to promote the polymerization of an otherwise secreted protein by a process requiring the function of the sortase A
-
-
?
additional information
?
-
-
two elements of Spa pilin precursor, the pilin motif and the sorting signal, are together sufficient to promote the polymerization of an otherwise secreted protein by a process requiring the function of the sortase A
-
-
?
additional information
?
-
-
sortase localization is facilitated by a positive charge that is necessary for efficient pilus biogenesis
-
-
?
additional information
?
-
-
non-gel proteomics is a powerful technique to rapidly identify sortase substrates and to gain insights on potential sorting motifs. LPXTG-containing proteins were identified exclusively in strains having a functional SrtA
-
-
?
additional information
?
-
the enzyme anchors surface proteins to the bacterial cell wall
-
-
?
additional information
?
-
-
the enzyme anchors surface proteins to the bacterial cell wall
-
-
?
additional information
?
-
-
the enzyme cleaves surface proteins of Staphylococcus aureus at the LPXT-/-G motif
-
-
?
additional information
?
-
-
the enzyme cleaves surface proteins of Staphylococcus aureus at the LPXT-/-G motif
-
-
?
additional information
?
-
-
transpeptidase activity. The enzyme catalyzes a cell wall sorting reaction in which a surface protein with a sorting signal containing a LPXT-/-G motif is cleaved between the Thr and Gly residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan. When a nucleophile is not available, sortase slowly hydrolyzes the LPET-/-G peptide at the same site. Ping-pong mechanism in which a common acyl-enzyme intermediate is formed in transpeptidation and hydrolysis. The nucleophile binding site of the enzyme is specific for diglycine. The S1' and S2' sites of the sortase both prefer a glycine residue, the S1' site is exclusively selective for glycine
-
-
?
additional information
?
-
-
transpeptidase activity: the enzyme catalyzes a cell wall sorting reaction in which a surface protein with a sorting signal containing a LPXT-/-G motif is cleaved between the Thr and Gly residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan. When a nucleophile is not available, sortase slowly hydrolyzes the LPETG peptide at the same site. Ping-pong mechanism in which a common acyl-enzyme intermediate is formed in transpeptidation and hydrolysis. The nucleophile binding site of the enzyme is specific for diglycine
-
-
?
additional information
?
-
the enzyme anchors surface proteins to the bacterial cells wall
-
-
?
additional information
?
-
-
the enzyme anchors surface proteins to the bacterial cells wall
-
-
?
additional information
?
-
-
the enzyme cleaves surface proteins of Staphylococcus aureus at the LPXT-/-G motif, catalyzes surface protein anchoring by means of a transpeptidation reaction that captures cleaved polypeptides as thioester enzyme intermediates
-
-
?
additional information
?
-
-
the enzyme cleaves surface proteins at the LPXTG motif and catalyzes the formation of an amide bond between the carboxyl group of Thr and the amino group of cell-wall crossbridges
-
-
?
additional information
?
-
-
gram-positive pathogenic bacteria display proteins on their surface that play important roles during infection. In Staphylococcus aureus theses surface proteins are anchored to the cell wall by two sortase, sortase A and sortaseB that recognize specific surface protein sorting signals. Sortase A is an essential virulence factor for establishment of septic arthritis
-
-
?
additional information
?
-
-
primary role of the SrtA isoform in Staphylococcus aureus adhesion and host colonization
-
-
?
additional information
?
-
-
the transpeptidase required for cell wall protein anchoring and virulence in Staphylococcus aureus
-
-
?
additional information
?
-
-
sortase A plays a role in the establishment of infections
-
-
?
additional information
?
-
-
sortase can transfer peptide substrates to oligosaccharides appended with a 6-deoxy-6-aminohexose moiety in a selective manner as that of an oligoglycine sequence
-
-
?
additional information
?
-
-
SrtA cleaves proteins at LPXTG-motif between threonine and glycine, and subsequently transfers the acyl-fragment to a N-terminal oligoglycine
-
-
?
additional information
?
-
-
SrtA recognizes LPXTG near the C-terminus of a target protein. The Cys184 of SrtA performs a nucleophilic attack at the peptide bond between T and G in LPXTG, resulting in a thioester intermediate with the carboxyl group of the C-terminal T linked to Cys184. This reactive intermediate reacts with the cross-bridge N-terminus of a cell-wall proteoglycan to anchor the target protein to the cell-wall peptidoglycan. SrtA accepts various peptide/protein substrates, so long as they bear the sorting signal LPXTG, and a range of amino nucleophiles
-
-
?
additional information
?
-
-
the enzyme cleaves the LPXTG sequence at the amide bond between the threonine and the glycine to form an acyl-enzyme complex. Nucleophilic attack by the amino group of the tri-glycine on the intermediate results in the formation of an LPXT-GGG bond and the liberation of the free enzyme
-
-
?
additional information
?
-
-
no activity with Dabcyl-KGIIPKTGGK-Edans, Dabcyl-KKVTIPQTGGIGT-Edans and Dabcyl-SFIPKTGM-Edans
-
-
?
additional information
?
-
-
sortase A also mediates transpeptidation reaction of indolicidin-derived peptides
-
-
?
additional information
?
-
-
sortase A mediates either head to tail cyclization or oligomerization and then head to tail cyclization of peptides (e.g. GGVTSAPDTLPKTGGS) and glycopeptides (e.g. MUC1 glycopeptide), depending on the peptide length, to produce 15-mer or higher cyclic peptides and glycopeptides
-
-
?
additional information
?
-
-
sortase A optimal cleavage site is LPETGG
-
-
?
additional information
?
-
-
sortase-mediated cyclization of histatin-1 (GG-histatin 1-LPETGG) provides a yield of more than 90%
-
-
?
additional information
?
-
-
truncated SrtADELTAN40 also catalyzes in vitro transpeptidation reaction
-
-
?
additional information
?
-
-
Surface proteins destined for cell wall anchoring contain a LPXTG sequence located in their C-terminus which serves as a substrate recognition motif for SrtA
-
-
?
additional information
?
-
-
the bacterial transpeptidase sortase A catalyzes the chemoselective ligation of peptides and proteins. During catalysis sortase A cleaves the conserved Leu-Pro-X-Thr-Gly sorting motif at the Thr residue under concomitant thioester formation at active site Cys184
-
-
?
additional information
?
-
-
the enzyme recognizes a 5-residue sequence motif, LPXTG, and cleaves the peptide bond between the Thr and Gly residues, forming an acyl enzyme intermediate between a cysteine at the active site of SrtA and the carboxylate at the truncated C-terminus of the substrate
-
-
?
additional information
?
-
-
semienzymatic cyclization of disulfide-rich peptides using sortase A, including the cyclotide kalata B1, alpha-conotoxin Vc1.1, and sunflower trypsin inhibitor 1, without the need for a thioester linker and using Fmoc chemistry, NMR spectral structure analysis, overview
-
-
?
additional information
?
-
-
the enzyme is highly selective and does not require any cofactors for the catalysis of protein ligation, but it is unable to access the recognition site within the highly structured regions of folded substrates. Ligation of purified glutathione-S-transferase and green fluorescence protein by recombinant circular enzyme
-
-
?
additional information
?
-
-
no activity with Dabcyl-KGIIPKTGGK-Edans, Dabcyl-KKVTIPQTGGIGT-Edans and Dabcyl-SFIPKTGM-Edans
-
-
?
additional information
?
-
-
truncated SrtADELTAN40 also catalyzes in vitro transpeptidation reaction
-
-
?
additional information
?
-
-
the enzyme is highly selective and does not require any cofactors for the catalysis of protein ligation, but it is unable to access the recognition site within the highly structured regions of folded substrates. Ligation of purified glutathione-S-transferase and green fluorescence protein by recombinant circular enzyme
-
-
?
additional information
?
-
-
sortase A plays a role in the establishment of infections
-
-
?
additional information
?
-
-
SrtA sortase of Streptococcus agalactiae is required for cell wall anchoring of proteins containing the LPXTG motif, for adhesion to epithelial cells, and for colonization of the mouse intestine
-
-
?
additional information
?
-
-
in addition to its role in processing LPXTG containing adhesins, sortase A has the function of contributing to transcriptional regulation of adhesin gene expression
-
-
?
additional information
?
-
-
role of srtA in adherence in vitro is dependent on capsule expression, the role of SrtA in adherence to human cells only being apparent in the absence of the pneumococcal capsule
-
-
?
additional information
?
-
-
SrtA is dispensable for pilus assembly and localization to the cell wall
-
-
?
additional information
?
-
-
SrtA contributes to antiopsonization in Streptococci. SrtA anchors surface adhesins as well as some proteins that function as antiopsonic molecules as a means of evading the human immune system. SrtA of Streptococcus sanguinis plays important roles in bacterial colonization
-
-
?
additional information
?
-
-
SrtA is involved in the virulence manifestation of streptococcal toxic shock syndrome
-
-
?
additional information
?
-
sortase A anchors the following proteins in the cell wall of Streptococcus uberis strain 0140J: putative fructan beta-fructosidase precursor, putative lactoferrin binding protein, putative collagen-like surface anchored protein, putative C5a peptidase precursor, and putative zinc-carboxypeptidase. Alternate cell wall anchoring motifs are either LPXTXD/E or LPXXXD
-
-
?
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(1E)-N'-[(1E)-(4-[(E)-[(diaminomethylene)hydrazono]methyl]phenyl)methylene]ethanehydrazonamide
-
-
(2-(trimethylammonium)ethyl)methanethiosulfonate
-
inhibition at 5 mM, inhibition is relieved by supplementing the reaction with 10 mM dithiothreitol
(2-methyl-1H-indol-3-yl)(oxo)acetic acid
-
-
(2-sulfonatoethyl)methanethiosulfonate
-
-
(2E)-2,3-bis(4-methoxyphenyl)acrylamide
-
IC50: 0.476 mM
(2E)-2,3-bis(4-methoxyphenyl)acrylonitrile
-
IC50: 0.187 mM
(2E)-2-(2-furoyl)-3-[(methyl[4-[(5-nitropyridin-2-yl)oxy]phenyl]oxido-l4-sulfanylidene)amino]acrylonitrile
-
-
(2E)-3-(2-furyl)-N-[3-(hydroxymethyl)-4-morpholin-4-ylphenyl]acrylamide
-
-
(2E)-3-[(methyl[4-[(5-nitropyridin-2-yl)oxy]phenyl]oxido-l4-sulfanylidene)amino]-2-(2-thienylcarbonyl)acrylonitrile
-
-
(2E)-4-([4-[(2-hydroxybenzoyl)amino]phenyl]amino)-4-oxobut-2-enoic acid
-
-
(2E)-N-(3-formyl-4-morpholin-4-ylphenyl)-3-(2-furyl)acrylamide
-
-
(2E)-N-(3-formyl-4-morpholin-4-ylphenyl)-3-(2-thienyl)acrylamide
-
-
(2E)-N-[3-(hydroxymethyl)-4-morpholin-4-ylphenyl]-3-(2-thienyl)acrylamide
-
-
(2Z)-2,3-bis(4-methoxyphenyl)acrylonitrile
-
IC50: 0.0279mM
(2Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
-
IC50: 0.009244 mM
(2Z)-3-(2-methoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
-
IC50: 0.0362 mM
(2Z)-3-(3,4-dimethoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
-
IC50: 0.02296 mM
(2Z)-3-(3,5-dimethoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
-
IC50: 0.025463 mM
(2Z)-3-(3-methoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
-
IC50: 0.0174 mM
(4E)-5-methyl-4-[[(4-nitrophenyl)amino]methylidene]-2-phenyl-2,4-dihydro-3H-pyrazole-3-thione
-
-
(5R)-3,5-bis(6-bromo-1H-indol-3-yl)-5,6-dihydropyrazin-2(1H)-one
-
IC50: 68.98 mg/L
(5Z)-3-(2,4-dimethylphenyl)-5-(3-nitrobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-(3-chlorophenyl)-5-(4-methyl-3-nitrobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-benzylidene-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-ethyl-5-(2-nitrobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-(2,4-dimethylphenyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-(3-chlorophenyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-(3-methylphenyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-(4-nitrophenyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-phenyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(3-bromo-4-hydroxy-5-nitrobenzylidene)-3-(2,4-dimethylphenyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(3-chlorobenzylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-benzylidene-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-benzylidene-3-methyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-benzylidene-3-propyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(6-hydroxy-1H-indol-3-yl)(oxo)acetic acid
-
-
(6-methoxy-1H-indol-3-yl)(oxo)acetic acid
-
-
(6-methyl-1H-inden-3-yl)[4-(6-methyl-1H-indol-3-yl)-1H-imidazol-2-yl]methanone
-
IC50: 15.67 mg/Ll
(6R)-3,6-bis(6-bromo-1H-indol-3-yl)-5,6-dihydropyrazin-2(1H)-one
-
IC50: 86.34 mg/L
(6R)-6-(6-bromo-1H-indol-3-yl)-3-(1H-indol-3-yl)-5,6-dihydropyrazin-2(1H)-one
-
IC50: 34.04 mg/L
(Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl) acrylonitrile
-
potential of this inhibitor for the treatment of Staphylococcus aureus infections
1,2-bis(5-hydroxy-1H-indol-3-yl)ethane-1,2-dione
-
-
1-(3,4-dichlorophenyl)-3-(dimethylamino)propan-1-one
-
-
1-(3-methoxyphenyl)-2,3,4,9-tetrahydro-1H-beta-carboline
-
-
1-(4-bromophenyl)-3-(3-methylpiperidin-1-yl)propan-1-one
-
-
1-(4-chlorophenyl)-3-morpholin-4-ylpropan-1-one
-
-
1-(4-fluorophenyl)-3-morpholin-4-ylpropan-1-one
-
-
1-(4-methoxyphenyl)-2,3,4,9-tetrahydro-1H-beta-carboline
-
-
1-(4-methylphenyl)-3-morpholin-4-ylpropan-1-one
-
-
1-(naphthalen-2-yl)-2,3,4,9-tetrahydro-1H-beta-carboline
-
-
1-pentyl-2,3,4,9-tetrahydro-1H-beta-carboline
-
-
1-phenyl-2,3,4,9-tetrahydro-1H-beta-carbolin-7-ol
-
-
1-phenyl-2,3,4,9-tetrahydro-1H-beta-carboline
-
-
1-phenyl-4,9-dihydro-3H-beta-carboline
-
-
1-[4-(2-aminopyrimidin-4-yl)phenyl]-3-(4-chlorophenyl)urea
-
-
1H-indol-3-yl(oxo)acetic acid
-
-
2,3,4,9-tetrahydro-1H-beta-carboline-1-carboxylic acid
-
-
2-(1-oxoisoindolin-2-yl)acetic acid
-
-
2-(1H-indol-3-yl)-2-oxo-N-phenylacetamide
-
-
2-(2-methyl-1H-indol-3-yl)-2-oxo-N-phenylacetamide
-
-
2-(3,5-dichlorophenyl)-4-(ethylsulfanyl)-5-sulfanylpyridazin-3(2H)-one
-
-
2-(3,5-dichlorophenyl)-5-ethoxy-4-sulfanylpyridazin-3(2H)-one
-
-
2-(3-bromophenyl)-4,5-dichloropyridazin-3(2H)-one
-
-
2-(3-bromophenyl)-4-(ethylsulfanyl)-5-sulfanylpyridazin-3(2H)-one
-
-
2-(3-bromophenyl)-4-chloro-5-ethoxypyridazin-3(2H)-one
-
-
2-(3-bromophenyl)-5-chloro-4-ethoxypyridazin-3(2H)-one
-
-
2-(3-bromophenyl)-5-chloro-4-methoxypyridazin-3(2H)-one
-
-
2-(3-chlorophenyl)-4-methoxy-5-sulfanylpyridazin-3(2H)-one
-
-
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-(tricyclo[3.3.1.13,7]dec-1-yl)acetamide
-
-
2-(4-nitrophenyl)-4,5-dichloropyridazin-3-one
-
-
2-(6-hydroxy-1H-indol-3-yl)-2-oxo-N-phenylacetamide
-
-
2-(6-methoxy-1H-indol-3-yl)-2-oxo-N-phenylacetamide
-
-
2-cyclohexyl-4-(ethylsulfanyl)-5-sulfanylpyridazin-3(2H)-one
-
-
2-ethyl-4-hydroxy-5-(methylsulfanyl)pyridazin-3(2H)-one
-
-
2-hydroxy-1-(5-hydroxy-1H-indol-3-yl)ethanone
-
-
2-hydroxy-N-[4-[([[(4-methylphenyl)sulfonyl]amino]carbonyl)amino]phenyl]benzamide
-
-
2-morpholin-4-yl-5-[[(2E)-3-(2-thienyl)prop-2-enoyl]amino]benzamide
-
-
2-phenyl-4,5-dichloro-pyridazin-3-one
-
-
3,3,3-trifluoro-1-(phenylsulfonyl)-1-propene
-
IC50: 0.19 mM, irreversible
3,5-bis[[2-(4-nitrophenyl)-2-oxoethyl]thio]isothiazole-4-carbonitrile
-
-
3-(2-aminoethyl)-1H-indol-5-ol
-
-
3-(3-oxo-1,2-benzothiazol-2(3H)-yl)propanoic acid
-
-
3-(dimethylamino)-1-(2-thienyl)propan-1-one
-
-
3-(dimethylamino)-1-(3-nitrophenyl)propan-1-one
-
-
3-anilino-1-(3-nitrophenyl)propan-1-one
-
-
4,5-dichloro-2-(3,5-dichlorophenyl)pyridazin-3(2H)-one
-
-
4,5-dichloro-2-(3-fluorophenyl)pyridazin-3(2H)-one
-
-
4,5-dichloro-2-(3-methylphenyl)pyridazin-3(2H)-one
-
-
4,5-dichloro-2-cyclohexylpyridazin-3(2H)-one
-
-
4-(benzyloxy)-5-hydroxy-2-phenylpyridazin-3(2H)-one
-
-
4-(ethylsulfanyl)-2-(3-fluorophenyl)-5-sulfanylpyridazin-3(2H)-one
-
-
4-(ethylsulfanyl)-2-(3-methylphenyl)-5-sulfanylpyridazin-3(2H)-one
-
-
4-(ethylsulfanyl)-2-(4-nitrophenyl)-5-sulfanylpyridazin-3(2H)-one
-
-
4-(ethylsulfanyl)-2-phenyl-5-sulfanylpyridazin-3(2H)-one
-
-
4-(ethylsulfanyl)-5-hydroxy-2-phenylpyridazin-3(2H)-one
-
-
4-chloro-2-(3,5-dichlorophenyl)-5-ethoxypyridazin-3(2H)-one
-
-
4-chloro-2-cyclohexyl-5-ethoxypyridazin-3(2H)-one
-
-
4-chloro-5-(methylsulfanyl)-2-phenylpyridazin-3(2H)-one
-
-
4-chloro-5-ethoxy-2-(3-fluorophenyl)pyridazin-3(2H)-one
-
-
4-chloro-5-ethoxy-2-(3-methylphenyl)pyridazin-3(2H)-one
-
-
4-chloro-5-ethoxy-2-(4-nitrophenyl)pyridazin-3(2H)-one
-
-
4-chloro-5-ethoxy-2-phenylpyridazin-3-one
-
-
4-ethoxy-2-phenyl-5-sulfanylpyridazin-3(2H)-one
-
-
4-ethoxy-5-(2-pyridyldithio)-2-phenylpyridazin-3-one
-
-
4-ethoxy-5-(methyldithio)-2-phenylpyridazin-3-one
-
-
4-ethoxy-5-mercapto-2-phenylpyridazin-3-one
-
-
4-hydroxy-5-(methylsulfanyl)-2-phenylpyridazin-3(2H)-one
-
-
4-hydroxymercuribenzoate
-
-
5-chloro-2-(3,5-dichlorophenyl)-4-ethoxypyridazin-3(2H)-one
-
-
5-chloro-2-(3,5-dichlorophenyl)-4-methoxypyridazin-3(2H)-one
-
-
5-chloro-2-(3-fluorophenyl)-4-methoxypyridazin-3(2H)-one
-
-
5-chloro-2-cyclohexyl-4-ethoxypyridazin-3(2H)-one
-
-
5-chloro-2-cyclohexyl-4-methoxypyridazin-3(2H)-one
-
-
5-chloro-4-ethoxy-2-(3-fluorophenyl)pyridazin-3(2H)-one
-
-
5-chloro-4-ethoxy-2-(3-methylphenyl)pyridazin-3(2H)-one
-
-
5-chloro-4-ethoxy-2-(4-nitrophenyl)pyridazin-3(2H)-one
-
-
5-chloro-4-ethoxy-2-phenylpyridazin-3-one
-
-
5-chloro-4-methoxy-2-(3-methylphenyl)pyridazin-3(2H)-one
-
-
5-chloro-4-methoxy-2-phenylpyridazin-3(2H)-one
-
-
5-ethoxy-2-(3-fluorophenyl)-4-sulfanylpyridazin-3(2H)-one
-
-
5-ethoxy-2-(3-methylphenyl)-4-sulfanylpyridazin-3(2H)-one
-
-
5-ethoxy-2-phenyl-4-sulfanylpyridazin-3(2H)-one
-
-
5-hydroxy-1H-indole-3-carbaldehyde
-
-
5-hydroxy-4-methoxy-2-phenylpyridazin-3(2H)-one
-
-
5-methoxy-2-phenyl-4-sulfanylpyridazin-3(2H)-one
-
-
5-[[(2E)-3-(2-furyl)prop-2-enoyl]amino]-2-morpholin-4-ylbenzoic acid
-
-
6-hydroxy-2,3,4,9-tetrahydro-1H-beta-carbolin-1-one
-
-
6-hydroxydihydro-beta-carboline
-
-
7-hydroxy-2,3,4,9-tetrahydro-1H-beta-carboline-1-carboxylic acid
-
-
7-methoxy-1-pentyl-2,3,4,9-tetrahydro-1H-beta-carboline
-
-
7-methoxy-1-phenyl-2,3,4,9-tetrahydro-1H-beta-carboline
-
-
7-methoxy-1-phenyl-4,9-dihydro-3H-beta-carboline
-
-
7-methoxy-2,3,4,9-tetrahydro-1H-beta-carboline-1-carboxylic acid
-
-
benzyloxycarbonyl-Leu-Pro-Ala-Thr-CH2Cl
-
irreversible inhibitor of recombinant enzyme
benzyloxycarbonyl-Leu-Pro-Ala-Thr-CHN2
-
irreversible inhibitor of recombinant enzyme
beta-sitosterol-3-O-glucopyranoside
bis(4-ethoxy-2-phenyl-5-pyridazyl)disulfide
-
-
cis-1,2-bis(phenylsulfonyl)ethylene
-
IC50: 0.00113 mM, irreversible
divinyl sulfone
-
IC50: 0.00106 mM, irreversible
ethyl 4-[3-(4-bromophenyl)-3-oxopropyl]piperazine-1-carboxylate
-
-
ethyl vinyl sulfone
-
IC50: 0.00471 mM, irreversible
galangin
-
IC50 for recombinant SrtA(DELTA24): 0.123 mM, no antibacterial activity against Staphylococcus aureus
galangin-3-methyl ether
-
IC50 for recombinant SrtA(DELTA24): 0.1179 mM, no antibacterial activity against Staphylococcus aureus
iodoacetamide
-
active site Cys184 of sortase A can be alkylated by iodoacetamide resulting in irreversible modified enzyme. The selenol and thiol of mutant Sec-sortase and mutant Hcy-sortase are sensitive to alkylation as well
isoaaptamine
-
the suppression of fibronectin-binding activity by isoaaptamine highlights its potential for the treatment of Staphylococcus aureus infections via inhibition of SrtA activity
isorhamnetin
-
IC50 for recombinant SrtA(DELTA24): 0.05886 mM, no antibacterial activity against Staphylococcus aureus
isorhamnetin 3-O-beta-D-rutinoside
-
-
kaempferol
-
IC50 for recombinant SrtA(DELTA24): 0.07794 mM, no antibacterial activity against Staphylococcus aureus
kaempferol-3-rutinoside
-
-
maltol 3-O-(4'-O-p-coumaroyl-6'-O-(3-hydroxy-3-methylglutaroyl))-beta-glucopyranoside
-
-
maltol-3-O-(4'-O-cis-p-coumaroyl-6'-O-(3-hydroxy-3-methylglutaroyl))-beta-glucopyranoside
-
-
methyl (2E)-2,3-bis(4-methoxyphenyl)acrylate
-
IC50: 0.231 mM
methyl (2S,3S,7aS)-2-ethenesulfonyl-5-oxo-3-phenyltetrahydropyrrolizine-7a-carboxylate
-
-
methyl (2S,3S,7aS)-2-ethenesulfonyl-5-oxo-3-pyridin-3-yl-tetrahydropyrrolizine-7a-carboxylate
-
-
methyl (2S,3S,7aS)-3-(3,4-dimethoxyphenyl)-2-ethenesulfonyl-5-oxotetrahydropyrrolizine-7a-carboxylate
-
-
methyl (2S,4S,5S)-4-ethenesulfonyl-2-(2-methoxycarbonylethyl)-5-pyridin-3-yl-pyrrolidine-2-carboxylate
-
-
methyl (2Z)-2,3-bis(4-methoxyphenyl)acrylate
-
IC50: 0.909 mM
methyl (4S,5S)-4-(ethenylsulfonyl)-5-(2-fluorophenyl)-L-prolinate
-
-
methyl (4S,5S)-4-(ethenylsulfonyl)-5-(3-fluorophenyl)-L-prolinate
-
-
methyl (4S,5S)-4-(ethenylsulfonyl)-5-phenyl-L-prolinate
-
-
methyl 1-aminoadamantan-3-carboxylate
-
-
methyl 2-morpholin-4-yl-5-[[(2E)-3-(2-thienyl)prop-2-enoyl]amino]benzoate
-
-
methyl 3-(3-(3-oxobenzo[d]isothiazol-2(3H)-yl)propanamido)adamantane-1-carboxylate
-
-
methyl 3-(3-(4-fluoro-3-oxobenzo[d]isothiazol-2(3H)-yl)propanamido)adamantane-1-carboxylate
-
-
methyl 4-[3-(dimethylamino)propanoyl]benzenesulfinate
-
-
methyl 5-hydroxy-1H-indole-3-carboxylate
-
-
methyl 5-[[(2E)-3-(2-furyl)prop-2-enoyl]amino]-2-morpholin-4-ylbenzoate
-
-
methyl vinyl sulfone
-
IC50: 0.00624 mM, irreversible
morin
-
IC50 for recombinant SrtA(DELTA24): 0.03739 mM, no antibacterial activity against Staphylococcus aureus
myricetin
-
IC50 for recombinant SrtA(DELTA24): 0.04403 mM, no antibacterial activity against Staphylococcus aureus
N'-(2-(3-oxobenzo[d]isothiazol-2(3H)-yl)acetyl)adamantane-1-carbohydrazide
-
-
N'-(3-(3-oxobenzo[d]isothiazol-2(3H)-yl)propanoyl)adamantane-1-carbohydrazide
-
-
N'-(3-(4-fluoro-3-oxobenzo[d]isothiazol-2(3H)-yl)propanoyl)adamantane-1-carbohydrazide
-
-
N-(3,5-dimethyladamantan-1-yl)-3-(3-oxobenzo[d]isothiazol-2(3H)-yl)acetamide
-
-
N-(3,5-dimethyladamantan-1-yl)-3-(3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
-
-
N-(3,5-dimethyladamantan-1-yl)-3-(4-fluoro-3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
-
-
N-(3-hydroxy-5,7-dimethyladamantan-1-yl)-2-(3-oxobenzo[d]isothiazol-2(3H)-yl)acetamide
-
-
N-(3-hydroxy-5,7-dimethyladamantan-1-yl)-3-(3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
-
-
N-(3-hydroxy-5,7-dimethyladamantan-1-yl)-3-(4-fluoro-3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
-
-
N-(3-hydroxyadamantan-1-yl)-3-(3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
-
-
N-(3-ydroxyadamantan-1-yl)-3-(4-fluoro-3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
-
-
N-(adamantan-1-yl)-3-(4-fluoro-3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
-
-
N-adamantan-1-yl-3-(3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
-
-
NH2-YALPE-AlaPsi(PO2H-CH2)Gly-EE-NH2
-
nonhydrolyzable phosphinic peptidomimetic inhibitor of SrtA derived from the LPXTG substrate sequence, simple reversible competitive inhibitor
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoic acid
-
-
psammaplin A1
-
potential of this inhibitor for the treatment of Staphylococcus aureus infections
quercetin
-
IC50 for recombinant SrtA(DELTA24): 0.0527 mM, no antibacterial activity against Staphylococcus aureus
quercetin-3,3'-dimethyl ether
-
IC50 for recombinant SrtA(DELTA24): 0.05361 mM, no antibacterial activity against Staphylococcus aureus
[2-(trimethylammonium)ethyl]methanethiosulfonate
-
the inhibitor interferes with the cleavage of sorting signals at the LPXTG motif
[4-(6-bromo-1H-indol-3-yl)-1H-imidazol-2-yl](1H-indol-3-yl)methanone
-
IC50: 19.44 mg/L
[4-(6-bromo-1H-indol-3-yl)-1H-imidazol-2-yl](6-hydroxy-1H-indol-3-yl)methanone
-
IC50: 16.7 mg/L
berberine chloride
-
potential of this inhibitor for the treatment of Staphylococcus aureus infections
beta-sitosterol-3-O-glucopyranoside
-
potential of this inhibitor for the treatment of Staphylococcus aureus infections
beta-sitosterol-3-O-glucopyranoside
-
-
beta-sitosterol-3-O-glucopyranoside
-
IC50: 18.3 mg/L
phenyl vinyl sulfone
-
IC50: 0.736 mM, irreversible
additional information
-
aryl (beta-amino)ethyl ketones inhibit sortase enzymes. Inhibition of sortases occurs through an irreversible, covalent modification of their active site cysteine. Sortases specifically activate this class of molecules via beta-elimination, generating a reactive olefin intermediate that covalently modifies the cysteine thiol
-
additional information
-
SrtA activity is a prime target for inhibition of Staphylococcus aureus colonization
-
additional information
-
no inhibition by (3R,6S)-3,6-bis(6-bromo-1H-indol-3-yl)piperazin-2-one and (3R,6S)-3,6-bis(6-bromo-1H-indol-3-yl)piperazin-2-one
-
additional information
-
no inhibition by phenyl trans-styryl sulfone
-
additional information
-
no inhibition by trans-stilbene
-
additional information
-
aryl (beta-amino)ethyl ketones inhibit sortase enzymes. Inhibition of sortases occurs through an irreversible, covalent modification of their active site cysteine. Sortases specifically activate this class of molecules via beta-elimination, generating a reactive olefin intermediate that covalently modifies the cysteine thiol
-
additional information
-
anti-SrtA serum inhibits Staphylococcus aureus biofilm formation
-
additional information
-
not inhibited by 3-nitropropionate
-
additional information
-
small molecule library screening, synthesis and analysis of irreversible benzisothiazolinone-based inhibitors of the enzyme, structure-activity relationship, overview. No inhibition by aminoadamantan, methyl 1-aminoadamantan-3-carboxylate, and 2-(1-oxoisoindolin-2-yl)acetic acid. Structure determination of inhibitor 1-SrtA complex using purified recombinant nontagged truncated enzyme mutant variant SrtADELTA59, NMR structure determination and analysis
-
additional information
-
sortase A inhibitory metabolites from the flowers of Sophora japonica, overview
-
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0.275
(1E)-N'-[(1E)-(4-[(E)-[(diaminomethylene)hydrazono]methyl]phenyl)methylene]ethanehydrazonamide
Staphylococcus aureus
-
-
0.133
(2-methyl-1H-indol-3-yl)(oxo)acetic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.476
(2E)-2,3-bis(4-methoxyphenyl)acrylamide
Staphylococcus aureus
-
IC50: 0.476 mM
0.187
(2E)-2,3-bis(4-methoxyphenyl)acrylonitrile
Staphylococcus aureus
-
IC50: 0.187 mM
0.15
(2E)-2-(2-furoyl)-3-[(methyl[4-[(5-nitropyridin-2-yl)oxy]phenyl]oxido-l4-sulfanylidene)amino]acrylonitrile
Staphylococcus aureus
-
-
0.111
(2E)-3-(2-furyl)-N-[3-(hydroxymethyl)-4-morpholin-4-ylphenyl]acrylamide
Staphylococcus aureus
-
-
0.4
(2E)-3-[(methyl[4-[(5-nitropyridin-2-yl)oxy]phenyl]oxido-l4-sulfanylidene)amino]-2-(2-thienylcarbonyl)acrylonitrile
Staphylococcus aureus
-
-
0.125
(2E)-4-([4-[(2-hydroxybenzoyl)amino]phenyl]amino)-4-oxobut-2-enoic acid
Staphylococcus aureus
-
-
0.107
(2E)-N-(3-formyl-4-morpholin-4-ylphenyl)-3-(2-furyl)acrylamide
Staphylococcus aureus
-
-
0.077
(2E)-N-(3-formyl-4-morpholin-4-ylphenyl)-3-(2-thienyl)acrylamide
Staphylococcus aureus
-
-
0.073
(2E)-N-[3-(hydroxymethyl)-4-morpholin-4-ylphenyl]-3-(2-thienyl)acrylamide
Staphylococcus aureus
-
-
0.0279
(2Z)-2,3-bis(4-methoxyphenyl)acrylonitrile
Staphylococcus aureus
-
IC50: 0.0279mM
0.009244
(2Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
Staphylococcus aureus
-
IC50: 0.009244 mM
0.0362
(2Z)-3-(2-methoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
Staphylococcus aureus
-
IC50: 0.0362 mM
0.02296
(2Z)-3-(3,4-dimethoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
Staphylococcus aureus
-
IC50: 0.02296 mM
0.025463
(2Z)-3-(3,5-dimethoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
Staphylococcus aureus
-
IC50: 0.025463 mM
0.0174
(2Z)-3-(3-methoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
Staphylococcus aureus
-
IC50: 0.0174 mM
0.0052
(4E)-5-methyl-4-[[(4-nitrophenyl)amino]methylidene]-2-phenyl-2,4-dihydro-3H-pyrazole-3-thione
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.119
(5Z)-3-(2,4-dimethylphenyl)-5-(3-nitrobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
1
(5Z)-3-(3-chlorophenyl)-5-(4-methyl-3-nitrobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
IC50 above 1.0 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.492
(5Z)-3-benzyl-5-benzylidene-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.104
(5Z)-3-ethyl-5-(2-nitrobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.0037
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-(2,4-dimethylphenyl)-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.017
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-(3-chlorophenyl)-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.015
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-(3-methylphenyl)-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.012
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-(4-nitrophenyl)-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.014
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-phenyl-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.035
(5Z)-5-(3-bromo-4-hydroxy-5-nitrobenzylidene)-3-(2,4-dimethylphenyl)-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.109
(5Z)-5-(3-chlorobenzylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.199
(5Z)-5-benzylidene-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.405
(5Z)-5-benzylidene-3-methyl-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.186
(5Z)-5-benzylidene-3-propyl-2-thioxo-1,3-thiazolidin-4-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.0896 - 0.736
1-(3,4-dichlorophenyl)-3-(dimethylamino)propan-1-one
0.0569 - 0.0837
1-(4-bromophenyl)-3-(3-methylpiperidin-1-yl)propan-1-one
0.0844 - 0.0906
1-(4-chlorophenyl)-3-morpholin-4-ylpropan-1-one
0.0472 - 0.0891
1-(4-fluorophenyl)-3-morpholin-4-ylpropan-1-one
0.0569 - 0.0889
1-(4-methylphenyl)-3-morpholin-4-ylpropan-1-one
0.0106
1-phenyl-2,3,4,9-tetrahydro-1H-beta-carbolin-7-ol
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.097
1-phenyl-4,9-dihydro-3H-beta-carboline
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.4
1-[4-(2-aminopyrimidin-4-yl)phenyl]-3-(4-chlorophenyl)urea
Staphylococcus aureus
-
-
0.069
1H-indol-3-yl(oxo)acetic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.174
2-(1H-indol-3-yl)-2-oxo-N-phenylacetamide
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.061
2-(2-methyl-1H-indol-3-yl)-2-oxo-N-phenylacetamide
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.301
2-(3,5-dichlorophenyl)-4-(ethylsulfanyl)-5-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.166
2-(3,5-dichlorophenyl)-5-ethoxy-4-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
2-(3-bromophenyl)-4,5-dichloropyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
2-(3-bromophenyl)-4-(ethylsulfanyl)-5-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
2-(3-bromophenyl)-4-chloro-5-ethoxypyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
2-(3-bromophenyl)-5-chloro-4-ethoxypyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
2-(3-bromophenyl)-5-chloro-4-methoxypyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.0045
2-(3-chlorophenyl)-4-methoxy-5-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.00611
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-(tricyclo[3.3.1.13,7]dec-1-yl)acetamide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA59
0.05
2-(4-nitrophenyl)-4,5-dichloropyridazin-3-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.0179
2-cyclohexyl-4-(ethylsulfanyl)-5-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
2-ethyl-4-hydroxy-5-(methylsulfanyl)pyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.226
2-hydroxy-N-[4-[([[(4-methylphenyl)sulfonyl]amino]carbonyl)amino]phenyl]benzamide
Staphylococcus aureus
-
-
0.105
2-morpholin-4-yl-5-[[(2E)-3-(2-thienyl)prop-2-enoyl]amino]benzamide
Staphylococcus aureus
-
-
0.05
2-phenyl-4,5-dichloro-pyridazin-3-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.19
3,3,3-trifluoro-1-(phenylsulfonyl)-1-propene
Staphylococcus aureus
-
IC50: 0.19 mM, irreversible
0.0973
3,5-bis[[2-(4-nitrophenyl)-2-oxoethyl]thio]isothiazole-4-carbonitrile
Staphylococcus aureus
-
-
0.0128
3-(3-oxo-1,2-benzothiazol-2(3H)-yl)propanoic acid
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA75
0.0548 - 0.0907
3-(dimethylamino)-1-(2-thienyl)propan-1-one
0.0543 - 0.0902
3-(dimethylamino)-1-(3-nitrophenyl)propan-1-one
0.066 - 0.0873
3-anilino-1-(3-nitrophenyl)propan-1-one
0.061
4,5-dichloro-2-(3,5-dichlorophenyl)pyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
4,5-dichloro-2-(3-fluorophenyl)pyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
4,5-dichloro-2-(3-methylphenyl)pyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
4,5-dichloro-2-cyclohexylpyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
4-(benzyloxy)-5-hydroxy-2-phenylpyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM,
0.0055
4-(ethylsulfanyl)-2-(3-fluorophenyl)-5-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.0033
4-(ethylsulfanyl)-2-(3-methylphenyl)-5-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.03
4-(ethylsulfanyl)-2-(4-nitrophenyl)-5-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.0014
4-(ethylsulfanyl)-2-phenyl-5-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
4-(ethylsulfanyl)-5-hydroxy-2-phenylpyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM,
0.05
4-chloro-2-(3,5-dichlorophenyl)-5-ethoxypyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
4-chloro-2-cyclohexyl-5-ethoxypyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
4-chloro-5-(methylsulfanyl)-2-phenylpyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
4-chloro-5-ethoxy-2-(3-fluorophenyl)pyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
4-chloro-5-ethoxy-2-(3-methylphenyl)pyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.219
4-chloro-5-ethoxy-2-(4-nitrophenyl)pyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.001
4-chloro-5-ethoxy-2-phenylpyridazin-3-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.0002
4-ethoxy-2-phenyl-5-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.013
4-ethoxy-5-mercapto-2-phenylpyridazin-3-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
4-hydroxy-5-(methylsulfanyl)-2-phenylpyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.1125
4-hydroxymercuribenzoate
Streptococcus mutans
-
pH and temperature not specified in the publication
0.05
5-chloro-2-(3,5-dichlorophenyl)-4-ethoxypyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
5-chloro-2-(3,5-dichlorophenyl)-4-methoxypyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
5-chloro-2-(3-fluorophenyl)-4-methoxypyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
5-chloro-2-cyclohexyl-4-ethoxypyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
5-chloro-2-cyclohexyl-4-methoxypyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
5-chloro-4-ethoxy-2-(3-fluorophenyl)pyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
5-chloro-4-ethoxy-2-(3-methylphenyl)pyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
5-chloro-4-ethoxy-2-(4-nitrophenyl)pyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
5-chloro-4-ethoxy-2-phenylpyridazin-3-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
5-chloro-4-methoxy-2-(3-methylphenyl)pyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
5-chloro-4-methoxy-2-phenylpyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.0057
5-ethoxy-2-(3-fluorophenyl)-4-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.0031
5-ethoxy-2-(3-methylphenyl)-4-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.0044
5-ethoxy-2-phenyl-4-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.05
5-hydroxy-4-methoxy-2-phenylpyridazin-3(2H)-one
Staphylococcus aureus
-
IC50 above 0.05 mM,
0.0093
5-methoxy-2-phenyl-4-sulfanylpyridazin-3(2H)-one
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.181
5-[[(2E)-3-(2-furyl)prop-2-enoyl]amino]-2-morpholin-4-ylbenzoic acid
Staphylococcus aureus
-
-
0.067
6-hydroxydihydro-beta-carboline
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0115
7-methoxy-1-phenyl-2,3,4,9-tetrahydro-1H-beta-carboline
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.025
7-methoxy-1-phenyl-4,9-dihydro-3H-beta-carboline
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0015
bis(4-ethoxy-2-phenyl-5-pyridazyl)disulfide
Staphylococcus aureus
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25°C
0.00113
cis-1,2-bis(phenylsulfonyl)ethylene
Staphylococcus aureus
-
IC50: 0.00113 mM, irreversible
0.0915
curcumin
Streptococcus mutans
-
pH and temperature not specified in the publication
0.00106
divinyl sulfone
Staphylococcus aureus
-
IC50: 0.00106 mM, irreversible
0.0802 - 0.0907
ethyl 4-[3-(4-bromophenyl)-3-oxopropyl]piperazine-1-carboxylate
0.00471
ethyl vinyl sulfone
Staphylococcus aureus
-
IC50: 0.00471 mM, irreversible
0.123
galangin
Staphylococcus aureus
-
IC50 for recombinant SrtA(DELTA24): 0.123 mM, no antibacterial activity against Staphylococcus aureus
0.1179
galangin-3-methyl ether
Staphylococcus aureus
-
IC50 for recombinant SrtA(DELTA24): 0.1179 mM, no antibacterial activity against Staphylococcus aureus
0.05886
isorhamnetin
Staphylococcus aureus
-
IC50 for recombinant SrtA(DELTA24): 0.05886 mM, no antibacterial activity against Staphylococcus aureus
0.0621
isorhamnetin 3-O-beta-D-rutinoside
Streptococcus mutans
-
pH and temperature not specified in the publication
0.07794
kaempferol
Staphylococcus aureus
-
IC50 for recombinant SrtA(DELTA24): 0.07794 mM, no antibacterial activity against Staphylococcus aureus
0.0607
kaempferol-3-rutinoside
Streptococcus mutans
-
pH and temperature not specified in the publication
0.0943
maltol 3-O-(4'-O-p-coumaroyl-6'-O-(3-hydroxy-3-methylglutaroyl))-beta-glucopyranoside
Streptococcus mutans
-
pH and temperature not specified in the publication
0.0586
maltol-3-O-(4'-O-cis-p-coumaroyl-6'-O-(3-hydroxy-3-methylglutaroyl))-beta-glucopyranoside
Streptococcus mutans
-
pH and temperature not specified in the publication
0.231
methyl (2E)-2,3-bis(4-methoxyphenyl)acrylate
Staphylococcus aureus
-
IC50: 0.231 mM
2.2
methyl (2S,3S,7aS)-2-ethenesulfonyl-5-oxo-3-phenyltetrahydropyrrolizine-7a-carboxylate
Staphylococcus aureus
-
pH 7.5, 37°C
2.47
methyl (2S,3S,7aS)-2-ethenesulfonyl-5-oxo-3-pyridin-3-yl-tetrahydropyrrolizine-7a-carboxylate
Staphylococcus aureus
-
pH 7.5, 37°C
2.68
methyl (2S,3S,7aS)-3-(3,4-dimethoxyphenyl)-2-ethenesulfonyl-5-oxotetrahydropyrrolizine-7a-carboxylate
Staphylococcus aureus
-
pH 7.5, 37°C
1.86
methyl (2S,4S,5S)-4-ethenesulfonyl-2-(2-methoxycarbonylethyl)-5-pyridin-3-yl-pyrrolidine-2-carboxylate
Staphylococcus aureus
-
pH 7.5, 37°C
0.909
methyl (2Z)-2,3-bis(4-methoxyphenyl)acrylate
Staphylococcus aureus
-
IC50: 0.909 mM
1.32
methyl (4S,5S)-4-(ethenylsulfonyl)-5-(2-fluorophenyl)-L-prolinate
Staphylococcus aureus
-
pH 7.5, 37°C
1.04
methyl (4S,5S)-4-(ethenylsulfonyl)-5-(3-fluorophenyl)-L-prolinate
Staphylococcus aureus
-
pH 7.5, 37°C
0.85
methyl (4S,5S)-4-(ethenylsulfonyl)-5-phenyl-L-prolinate
Staphylococcus aureus
-
pH 7.5, 37°C
0.071
methyl 2-morpholin-4-yl-5-[[(2E)-3-(2-thienyl)prop-2-enoyl]amino]benzoate
Staphylococcus aureus
-
-
0.00508
methyl 3-(3-(3-oxobenzo[d]isothiazol-2(3H)-yl)propanamido)adamantane-1-carboxylate
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA66
0.00506
methyl 3-(3-(4-fluoro-3-oxobenzo[d]isothiazol-2(3H)-yl)propanamido)adamantane-1-carboxylate
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA71
0.0698 - 0.0913
methyl 4-[3-(dimethylamino)propanoyl]benzenesulfinate
0.058
methyl 5-[[(2E)-3-(2-furyl)prop-2-enoyl]amino]-2-morpholin-4-ylbenzoate
Staphylococcus aureus
-
-
0.00624
methyl vinyl sulfone
Staphylococcus aureus
-
IC50: 0.00624 mM, irreversible
0.03739
morin
Staphylococcus aureus
-
IC50 for recombinant SrtA(DELTA24): 0.03739 mM, no antibacterial activity against Staphylococcus aureus
0.04403
myricetin
Staphylococcus aureus
-
IC50 for recombinant SrtA(DELTA24): 0.04403 mM, no antibacterial activity against Staphylococcus aureus
0.0038
N'-(2-(3-oxobenzo[d]isothiazol-2(3H)-yl)acetyl)adamantane-1-carbohydrazide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA72
0.00422
N'-(3-(3-oxobenzo[d]isothiazol-2(3H)-yl)propanoyl)adamantane-1-carbohydrazide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA73
0.00339
N'-(3-(4-fluoro-3-oxobenzo[d]isothiazol-2(3H)-yl)propanoyl)adamantane-1-carbohydrazide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA74
0.00499
N-(3,5-dimethyladamantan-1-yl)-3-(3-oxobenzo[d]isothiazol-2(3H)-yl)acetamide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA60
0.00462
N-(3,5-dimethyladamantan-1-yl)-3-(3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA63
0.0041
N-(3,5-dimethyladamantan-1-yl)-3-(4-fluoro-3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA68
0.00387
N-(3-hydroxy-5,7-dimethyladamantan-1-yl)-2-(3-oxobenzo[d]isothiazol-2(3H)-yl)acetamide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA61
0.00706
N-(3-hydroxy-5,7-dimethyladamantan-1-yl)-3-(3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA64
0.00396
N-(3-hydroxy-5,7-dimethyladamantan-1-yl)-3-(4-fluoro-3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA69
0.00644
N-(3-hydroxyadamantan-1-yl)-3-(3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA65
0.00626
N-(3-ydroxyadamantan-1-yl)-3-(4-fluoro-3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA70
0.00401
N-(adamantan-1-yl)-3-(4-fluoro-3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA67
0.00381
N-adamantan-1-yl-3-(3-oxobenzo[d]isothiazol-2(3H)-yl)propanamide
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA62
0.042
p-hydroxymercuribenzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0169 - 0.736
phenyl vinyl sulfone
0.0527
quercetin
Staphylococcus aureus
-
IC50 for recombinant SrtA(DELTA24): 0.0527 mM, no antibacterial activity against Staphylococcus aureus
0.05361
quercetin-3,3'-dimethyl ether
Staphylococcus aureus
-
IC50 for recombinant SrtA(DELTA24): 0.05361 mM, no antibacterial activity against Staphylococcus aureus
additional information
additional information
Staphylococcus aureus
-
IC50 for aaptamine is 0.0235 mg/ml, IC50 for isoaaptamine is 0.0037 mg/ml, IC50 for demethylaaptamine is 0.0172 mg/ml, IC50 for demethyloxyaaptamine is 0.0201 mg/ml, IC50 for berberine chloride is 0.0087 mg/ml
-
0.0896
1-(3,4-dichlorophenyl)-3-(dimethylamino)propan-1-one
Staphylococcus aureus
-
-
0.0904
1-(3,4-dichlorophenyl)-3-(dimethylamino)propan-1-one
Staphylococcus aureus
-
-
0.736
1-(3,4-dichlorophenyl)-3-(dimethylamino)propan-1-one
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA75
0.0569
1-(4-bromophenyl)-3-(3-methylpiperidin-1-yl)propan-1-one
Staphylococcus aureus
-
-
0.0837
1-(4-bromophenyl)-3-(3-methylpiperidin-1-yl)propan-1-one
Staphylococcus aureus
-
-
0.0844
1-(4-chlorophenyl)-3-morpholin-4-ylpropan-1-one
Staphylococcus aureus
-
-
0.0906
1-(4-chlorophenyl)-3-morpholin-4-ylpropan-1-one
Staphylococcus aureus
-
-
0.0472
1-(4-fluorophenyl)-3-morpholin-4-ylpropan-1-one
Staphylococcus aureus
-
-
0.0891
1-(4-fluorophenyl)-3-morpholin-4-ylpropan-1-one
Staphylococcus aureus
-
-
0.0569
1-(4-methylphenyl)-3-morpholin-4-ylpropan-1-one
Staphylococcus aureus
-
-
0.0889
1-(4-methylphenyl)-3-morpholin-4-ylpropan-1-one
Staphylococcus aureus
-
-
0.0548
3-(dimethylamino)-1-(2-thienyl)propan-1-one
Staphylococcus aureus
-
-
0.0907
3-(dimethylamino)-1-(2-thienyl)propan-1-one
Staphylococcus aureus
-
-
0.0543
3-(dimethylamino)-1-(3-nitrophenyl)propan-1-one
Staphylococcus aureus
-
-
0.0902
3-(dimethylamino)-1-(3-nitrophenyl)propan-1-one
Staphylococcus aureus
-
-
0.066
3-anilino-1-(3-nitrophenyl)propan-1-one
Staphylococcus aureus
-
-
0.0873
3-anilino-1-(3-nitrophenyl)propan-1-one
Staphylococcus aureus
-
-
0.0802
ethyl 4-[3-(4-bromophenyl)-3-oxopropyl]piperazine-1-carboxylate
Staphylococcus aureus
-
-
0.0907
ethyl 4-[3-(4-bromophenyl)-3-oxopropyl]piperazine-1-carboxylate
Staphylococcus aureus
-
-
0.0698
methyl 4-[3-(dimethylamino)propanoyl]benzenesulfinate
Staphylococcus aureus
-
-
0.0913
methyl 4-[3-(dimethylamino)propanoyl]benzenesulfinate
Staphylococcus aureus
-
-
0.0169
phenyl vinyl sulfone
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant His6-tagged truncated enzyme mutant variant SrtADELTA75
0.736
phenyl vinyl sulfone
Staphylococcus aureus
-
IC50: 0.736 mM, irreversible
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Staphylococcus aureus
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Staphylococcus aureus sortase transpeptidase SrtA: insight into the kinetic mechanism and evidence for a reverse protonation catalytic mechanism
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Staphylococcus aureus
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Staphylococcus aureus, Staphylococcus aureus Newman
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Staphylococcus aureus
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The SrtA sortase of Streptococcus agalactiae is required for cell wall anchoring of proteins containing the LPXTG motif, for adhesion to epithelial cells, and for colonization of the mouse intestine
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2005
Streptococcus agalactiae
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Zink, S.D.; Burns, D.L.
Importance of srtA and srtB for growth of Bacillus anthracis in macrophages
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2005
Bacillus anthracis
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Vinyl sulfones: inhibitors of SrtA, a transpeptidase required for cell wall protein anchoring and virulence in Staphylococcus aureus
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Staphylococcus aureus
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Staphylococcus aureus, Staphylococcus aureus Newman
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Staphylococcus aureus
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Staphylococcus aureus sortase A transpeptidase. Calcium promotes sorting signal binding by altering the mobility and structure of an active site loop
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Staphylococcus aureus
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Discovery of diarylacrylonitriles as a novel series of small molecule sortase A inhibitors
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2004
Staphylococcus aureus
brenda
Ton-That, H.; Marraffini, L.A.; Schneewind, O.
Sortases and pilin elements involved in pilus assembly of Corynebacterium diphtheriae
Mol. Microbiol.
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2004
Corynebacterium diphtheriae
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Pucciarelli, M.G.; Calvo, E.; Sabet, C.; Bierne, H.; Cossart, P.; Garcia-del Portillo, F.
Identification of substrates of the Listeria monocytogenes sortases A and B by a non-gel proteomic analysis
Proteomics
5
4808-4817
2005
Listeria monocytogenes
brenda
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Inhibition of the Staphylococcus aureus sortase transpeptidase SrtA by phosphinic peptidomimetics
Bioorg. Med. Chem.
12
3723-3729
2004
Staphylococcus aureus
brenda
Chen, S.; Paterson, G.K.; Tong, H.H.; Mitchell, T.J.; DeMaria, T.F.
Sortase A contributes to pneumococcal nasopharyngeal colonization in the chinchilla model
FEMS Microbiol. Lett.
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2005
Streptococcus pneumoniae
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Gaspar, A.H.; Marraffini, L.A.; Glass, E.M.; Debord, K.L.; Ton-That, H.; Schneewind, O.
Bacillus anthracis sortase A (SrtA) anchors LPXTG motif-containing surface proteins to the cell wall envelope
J. Bacteriol.
187
4646-4655
2005
Bacillus anthracis
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Aulabaugh, A.; Ding, W.; Kapoor, B.; Tabei, K.; Alksne, L.; Dushin, R.; Zatz, T.; Ellestad, G.; Huang, X.
Development of an HPLC assay for Staphylococcus aureus sortase: evidence for the formation of the kinetically competent acyl enzyme intermediate
Anal. Biochem.
360
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2007
Staphylococcus aureus
brenda
Frankel, B.A.; Tong, Y.; Bentley, M.L.; Fitzgerald, M.C.; McCafferty, D.G.
Mutational analysis of active site residues in the Staphylococcus aureus transpeptidase SrtA
Biochemistry
46
7269-7278
2007
Staphylococcus aureus
brenda
Lu, C.; Zhu, J.; Wang, Y.; Umeda, A.; Cowmeadow, R.B.; Lai, E.; Moreno, G.N.; Person, M.D.; Zhang, Z.
Staphylococcus aureus sortase A exists as a dimeric protein in vitro
Biochemistry
46
9346-9354
2007
Staphylococcus aureus
brenda
Zhu, J.; Lu, C.; Standland, M.; Lai, E.; Moreno, G.N.; Umeda, A.; Jia, X.; Zhang, Z.
Single mutation on the surface of Staphylococcus aureus sortase A can disrupt its dimerization
Biochemistry
47
1667-1674
2008
Staphylococcus aureus
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Parthasarathy, R.; Subramanian, S.; Boder, E.T.
Sortase A as a novel molecular "stapler" for sequence-specific protein conjugation
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2007
Staphylococcus aureus
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Jang, K.H.; Chung, S.C.; Shin, J.; Lee, S.H.; Kim, T.I.; Lee, H.S.; Oh, K.B.
Aaptamines as sortase A inhibitors from the tropical sponge Aaptos aaptos
Bioorg. Med. Chem. Lett.
17
5366-5369
2007
Staphylococcus aureus
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Chenna, B.C.; Shinkre, B.A.; King, J.R.; Lucius, A.L.; Narayana, S.V.; Velu, S.E.
Identification of novel inhibitors of bacterial surface enzyme Staphylococcus aureus sortase A
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2008
Staphylococcus aureus
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Tanaka, T.; Yamamoto, T.; Tsukiji, S.; Nagamune, T.
Site-specific protein modification on living cells catalyzed by Sortase
Chembiochem
9
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2008
Staphylococcus aureus
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Samantaray, S.; Marathe, U.; Dasgupta, S.; Nandicoori, V.K.; Roy, R.P.
Peptide-sugar ligation catalyzed by transpeptidase sortase: A facile approach to neoglycoconjugate synthesis
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2008
Staphylococcus aureus
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Maresso, A.W.; Wu, R.; Kern, J.W.; Zhang, R.; Janik, D.; Missiakas, D.M.; Duban, M.; Joachimiak, A.; Schneewind, O.
Activation of inhibitors by sortase triggers irreversible modification of the active site
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Bacillus anthracis, Staphylococcus aureus
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Engineering the substrate specificity of Staphylococcus aureus sortase A. The beta6/beta7 loop from SrtB confers NPQTN recognition to SrtA
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Staphylococcus aureus
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Mutagenesis studies of substrate recognition and catalysis in the sortase A transpeptidase from Staphylococcus aureus
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Staphylococcus aureus
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Josefsson, E.; Kubica, M.; Mydel, P.; Potempa, J.; Tarkowski, A.
In vivo sortase A and clumping factor A mRNA expression during Staphylococcus aureus infection
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2008
Staphylococcus aureus
brenda
Paterson, G.K.; Mitchell, T.J.
The role of Streptococcus pneumoniae sortase A in colonization and pathogenesis
Microbes Infect.
8
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2006
Streptococcus pneumoniae
brenda
Yamaguchi, M.; Terao, Y.; Ogawa, T.; Takahashi, T.; Hamada, S.; Kawabata, S.
Role of Streptococcus sanguinis sortase A in bacterial colonization
Microbes Infect.
8
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2006
Streptococcus sanguinis
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Nobbs, A.H.; Vajna, R.M.; Johnson, J.R.; Zhang, Y.; Erlandsen, S.L.; Oli, M.W.; Kreth, J.; Brady, L.J.; Herzberg, M.C.
Consequences of a sortase A mutation in Streptococcus gordonii
Microbiology
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2007
Streptococcus gordonii
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Wang, C.; Li, M.; Feng, Y.; Zheng, F.; Dong, Y.; Pan, X.; Cheng, G.; Dong, R.; Hu, D.; Feng, X.; Ge, J.; Liu, D.; Wang, J.; Cao, M.; Hu, F.; Tang, J.
The involvement of sortase A in high virulence of STSS-causing Streptococcus suis serotype 2
Arch. Microbiol.
191
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2009
Streptococcus suis
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Kudryavtsev, K.V.; Bentley, M.L.; McCafferty, D.G.
Probing of the cis-5-phenyl proline scaffold as a platform for the synthesis of mechanism-based inhibitors of the Staphylococcus aureus sortase SrtA isoform
Bioorg. Med. Chem.
17
2886-2893
2009
Staphylococcus aureus
brenda
Clow, F.; Fraser, J.D.; Proft, T.
Immobilization of proteins to biacore sensor chips using Staphylococcus aureus sortase A
Biotechnol. Lett.
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1603-1607
2008
Staphylococcus aureus
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LeMieux, J.; Woody, S.; Camilli, A.
Roles of the sortases of Streptococcus pneumoniae in assembly of the RlrA pilus
J. Bacteriol.
190
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2008
Streptococcus pneumoniae
brenda
Kline, K.A.; Kau, A.L.; Chen, S.L.; Lim, A.; Pinkner, J.S.; Rosch, J.; Nallapareddy, S.R.; Murray, B.E.; Henriques-Normark, B.; Beatty, W.; Caparon, M.G.; Hultgren, S.J.
Mechanism for sortase localization and role in efficient pilus assembly in Enterococcus faecalis
J. Bacteriol.
191
3237-3247
2009
Enterococcus faecalis
brenda
Race, P.R.; Bentley, M.L.; Melvin, J.A.; Crow, A.; Hughes, R.K.; Smith, W.D.; Sessions, R.B.; Kehoe, M.A.; McCafferty, D.G.; Banfield, M.J.
Crystal structure of Streptococcus pyogenes sortase A: implications for sortase mechanism
J. Biol. Chem.
284
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2009
Streptococcus pyogenes (Q99ZN4), Streptococcus pyogenes, Streptococcus pyogenes SF370 (Q99ZN4)
brenda
Pritz, S.; Wolf, Y.; Kraetke, O.; Klose, J.; Bienert, M.; Beyermann, M.
Enzymatic ligation of peptides, peptide nucleic acids and proteins by means of sortase A
Adv. Exp. Med. Biol.
611
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2009
Staphylococcus aureus
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Xiong, N.; Hu, C.; Zhang, Y.; Chen, S.
Interaction of sortase A and lipase 2 in the inhibition of Staphylococcus aureus biofilm formation
Arch. Microbiol.
191
879-884
2009
Staphylococcus aureus, Staphylococcus aureus ATCC 25923
brenda
Ito, T.; Sadamoto, R.; Naruchi, K.; Togame, H.; Takemoto, H.; Kondo, H.; Nishimura, S.
Highly oriented recombinant glycosyltransferases: site-specific immobilization of unstable membrane proteins by using Staphylococcus aureus sortase A
Biochemistry
49
2604-2614
2010
Staphylococcus aureus
brenda
Suree, N.; Yi, S.W.; Thieu, W.; Marohn, M.; Damoiseaux, R.; Chan, A.; Jung, M.E.; Clubb, R.T.
Discovery and structure-activity relationship analysis of Staphylococcus aureus sortase A inhibitors
Bioorg. Med. Chem.
17
7174-7185
2009
Staphylococcus aureus
brenda
Gianfaldoni, C.; Maccari, S.; Pancotto, L.; Rossi, G.; Hilleringmann, M.; Pansegrau, W.; Sinisi, A.; Moschioni, M.; Masignani, V.; Rappuoli, R.; Del Giudice, G.; Ruggiero, P.
Sortase A confers protection against Streptococcus pneumoniae in mice
Infect. Immun.
77
2957-2961
2009
Streptococcus pneumoniae, Streptococcus pneumoniae TIGR4, Streptococcus pneumoniae D39
brenda
Guiton, P.S.; Hung, C.S.; Kline, K.A.; Roth, R.; Kau, A.L.; Hayes, E.; Heuser, J.; Dodson, K.W.; Caparon, M.G.; Hultgren, S.J.
Contribution of autolysin and sortase A during Enterococcus faecalis DNA-dependent biofilm development
Infect. Immun.
77
3626-3638
2009
Enterococcus faecalis
brenda
Wu, Z.; Guo, X.; Wang, Q.; Swarts, B.M.; Guo, Z.
Sortase A-catalyzed transpeptidation of glycosylphosphatidylinositol derivatives for chemoenzymatic synthesis of GPI-anchored proteins
J. Am. Chem. Soc.
132
1567-1571
2010
Staphylococcus aureus
brenda
Weiner, E.M.; Robson, S.A.; Marohn, M.; Clubb, R.T.
The sortase A enzyme that attaches proteins to the cell wall of Bacillus anthracis contains an unusual active site architecture
J. Biol. Chem.
285
23433-23443
2010
Bacillus anthracis
brenda
Egan, S.A.; Kurian, D.; Ward, P.N.; Hunt, L.; Leigh, J.A.
Identification of sortase A (SrtA) substrates in Streptococcus uberis: evidence for an additional hexapeptide (LPXXXD) sorting motif
J. Proteome Res.
9
1088-1095
2010
Streptococcus uberis 0140J (B9DS55)
brenda
Lee, Y.J.; Han, Y.R.; Park, W.; Nam, S.H.; Oh, K.B.; Lee, H.S.
Synthetic analogs of indole-containing natural products as inhibitors of sortase A and isocitrate lyase
Bioorg. Med. Chem. Lett.
20
6882-6885
2010
Staphylococcus aureus
brenda
Dieye, Y.; Oxaran, V.; Ledue-Clier, F.; Alkhalaf, W.; Buist, G.; Juillard, V.; Lee, C.W.; Piard, J.C.
Functionality of sortase A in Lactococcus lactis
Appl. Environ. Microbiol.
76
7332-7337
2010
Lactococcus lactis, Lactococcus lactis IL1403
brenda
Wu, Z.; Guo, X.; Guo, Z.
Sortase A-catalyzed peptide cyclization for the synthesis of macrocyclic peptides and glycopeptides
Chem. Commun. (Camb. )
47
9218-9220
2011
Staphylococcus aureus
brenda
Bolscher, J.; Oudhoff, M.; Nazmi, K.; Antos, J.; Guimaraes, C.; Spooner, E.; Haney, E.; Garcia Vallejo, J.; Vogel, H.; Vant Hof, W.; Ploegh, H.; Veerman, E.
Sortase A as a tool for high-yield histatin cyclization
FASEB J.
25
2650-2658
2011
Staphylococcus aureus
brenda
Piotukh, K.; Geltinger, B.; Heinrich, N.; Gerth, F.; Beyermann, M.; Freund, C.; Schwarzer, D.
Directed evolution of sortase A mutants with altered substrate selectivity profiles
J. Am. Chem. Soc.
133
17536-17539
2011
Staphylococcus aureus
brenda
Dasgupta, S.; Samantaray, S.; Sahal, D.; Roy, R.P.
Isopeptide ligation catalyzed by quintessential sortase A: mechanistic cues from cyclic and branched oligomers of indolicidin
J. Biol. Chem.
286
23996-24006
2011
Staphylococcus aureus
brenda
Levary, D.A.; Parthasarathy, R.; Boder, E.T.; Ackerman, M.E.
Protein-protein fusion catalyzed by sortase A
PLoS ONE
6
e18342
2011
Staphylococcus sp.
brenda
Khare, B.; Krishnan, V.; Rajashankar, K.R.; I-Hsiu, H.; Xin, M.; Ton-That, H.; Narayana, S.V.
Structural differences between the Streptococcus agalactiae housekeeping and pilus-specific sortases: SrtA and SrtC1
PLoS ONE
6
e22995
2011
Streptococcus agalactiae (Q8DZY1), Streptococcus agalactiae, Streptococcus agalactiae 2603 V/R (Q8DZY1)
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Sortase A substrate specificity in GBS pilus 2a cell wall anchoring
PLoS ONE
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2011
Staphylococcus aureus, Staphylococcus aureus 515
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Tian, B.; Eriksson, L.
Structural changes of Listeria monocytogenes sortase A: A key to understanding the catalytic mechanism
Proteins
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1564-1572
2011
Listeria monocytogenes
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Zhulenkovs, D.; Jaudzems, K.; Zajakina, A.; Leonchiks, A.
Enzymatic activity of circular sortase A under denaturing conditions: an advanced tool for protein ligation
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2014
Staphylococcus aureus, Staphylococcus aureus MSSA476
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brenda
Biswas, T.; Pawale, V.S.; Choudhury, D.; Roy, R.P.
Sorting of LPXTG peptides by archetypal sortase A: role of invariant substrate residues in modulating the enzyme dynamics and conformational signature of a productive substrate
Biochemistry
53
2515-2524
2014
Staphylococcus aureus
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Heck, T.; Pham, P.H.; Hammes, F.; Thoeny-Meyer, L.; Richter, M.
Continuous monitoring of enzymatic reactions on surfaces by real-time flow cytometry: sortase a catalyzed protein immobilization as a case study
Bioconjug. Chem.
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1492-1500
2014
Staphylococcus aureus
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Yang, W.Y.; Won, T.H.; Ahn, C.H.; Lee, S.H.; Yang, H.C.; Shin, J.; Oh, K.B.
Streptococcus mutans sortase A inhibitory metabolites from the flowers of Sophora japonica
Bioorg. Med. Chem. Lett.
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1394-1397
2015
Streptococcus mutans
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Zhulenkovs, D.; Rudevica, Z.; Jaudzems, K.; Turks, M.; Leonchiks, A.
Discovery and structure-activity relationship studies of irreversible benzisothiazolinone-based inhibitors against Staphylococcus aureus sortase A transpeptidase
Bioorg. Med. Chem.
22
5988-6003
2014
Staphylococcus aureus
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Schmohl, L.; Wagner, F.R.; Schuemann, M.; Krause, E.; Schwarzer, D.
Semisynthesis and initial characterization of sortase A mutants containing selenocysteine and homocysteine
Bioorg. Med. Chem.
23
2883-2889
2015
Staphylococcus aureus
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Chen, F.; Liu, B.; Wang, D.; Wang, L.; Deng, X.; Bi, C.; Xiong, Y.; Wu, Q.; Cui, Y.; Zhang, Y.; Li, X.; Wang, Y.; Liu, B.; Cao, Y.
Role of sortase A in the pathogenesis of Staphylococcus aureus-induced mastitis in mice
FEMS Microbiol. Lett.
351
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2014
Staphylococcus aureus, Staphylococcus aureus Newman D2C
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Wang, J.; Zou, L.L.; Li, A.X.
Construction of a Streptococcus iniae sortase A mutant and evaluation of its potential as an attenuated modified live vaccine in Nile tilapia (Oreochromis niloticus)
Fish Shellfish Immunol.
40
392-398
2014
Streptococcus iniae (M1L099), Streptococcus iniae, Streptococcus iniae TBY-1 (M1L099)
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Jia, X.; Kwon, S.; Wang, C.I.; Huang, Y.H.; Chan, L.Y.; Tan, C.C.; Rosengren, K.J.; Mulvenna, J.P.; Schroeder, C.I.; Craik, D.J.
Semienzymatic cyclization of disulfide-rich peptides using sortase A
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2014
Staphylococcus aureus
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Kappel, K.; Wereszczynski, J.; Clubb, R.T.; McCammon, J.A.
The binding mechanism, multiple binding modes, and allosteric regulation of Staphylococcus aureus sortase A probed by molecular dynamics simulations
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1858-1871
2012
Staphylococcus aureus (Q95446), Staphylococcus aureus
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Kuropka, B.; Royla, N.; Freund, C.; Krause, E.
Sortase A mediated site-specific immobilization for identification of protein interactions in affinity purification-mass spectrometry experiments
Proteomics
15
1230-1234
2015
Staphylococcus aureus
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