Information on EC 3.4.22.70 - sortase A

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
3.4.22.70
-
RECOMMENDED NAME
GeneOntology No.
sortase A
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
The enzyme catalyses a cell wall sorting reaction in which a surface protein with a sorting signal containing a LPXTG 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.
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C60.001
-
-
-
-
sortase A transpeptidase
-
-
sortase SrtA
-
-
sortase transpeptidase
-
-
SrtA
-
-
-
-
SrtA
Lactococcus lactis IL1403
-
-
-
SrtA
Staphylococcus aureus 515, Staphylococcus aureus ATCC25923
-
-
-
SrtA protein
-
-
-
-
SrtA sortase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9033-39-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
parent strain Sterne 34F2
-
-
Manually annotated by BRENDA team
Lactococcus lactis IL1403
-
-
-
Manually annotated by BRENDA team
ATCC 6538p, recombinantly expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
SrtADELTAN, a soluble enzyme lacking the N-terminal signal peptide, residues 2-29 of SrtA and SrtDELTAN59, which contains only the presumed catalytic core
-
-
Manually annotated by BRENDA team
strain ATCC25923
-
-
Manually annotated by BRENDA team
Staphylococcus aureus 515
-
-
-
Manually annotated by BRENDA team
Staphylococcus aureus ATCC25923
strain ATCC25923
-
-
Manually annotated by BRENDA team
Staphylococcus aureus Newman
strain Newman
-
-
Manually annotated by BRENDA team
35B-SME15 (serotype 35B)
-
-
Manually annotated by BRENDA team
serotype 2, strain D39
-
-
Manually annotated by BRENDA team
strain TIGR4
-
-
Manually annotated by BRENDA team
strain SF370
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes SF370
strain SF370
UniProt
Manually annotated by BRENDA team
serotype 2
-
-
Manually annotated by BRENDA team
ATCC BAA-854/0140J
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
deletion of srtA affects the attachment stage and results in a deficiency in biofilm production, deletion of srtA has no effect on cell viability and cell growth
physiological function
-
intraperitoneal immunization with recombinant SrtA confers to mice protection against Streptococcus pneumoniae intraperitoneal challenge
physiological function
-
Bacillus anthracis uses the sortase A enzyme to anchor proteins to its cell wall envelope during vegetative growth
physiological function
-
the enzyme is responsible for the cell wall anchoring of LPXTG-containing proteins
physiological function
-
the enzyme catalyzes the covalent anchoring of surface proteins to the cell wall by linking the threonyl carboxylate of the LPXTG recognition motif to the amino group of the pentaglycine cross-bridge of the peptidoglycan
physiological function
-
sortase A covalently attaches proteins to the bacterial cell wall by cleaving between threonine and glycine at an LPXTG recognition motif
physiological function
Q8DZY1
sortase A is involved in cell wall anchoring of pilus polymers
physiological function
-
sortase A catalyzes cell wall anchoring reaction of LPXTG surface proteins
physiological function
Lactococcus lactis IL1403
-
the enzyme is responsible for the cell wall anchoring of LPXTG-containing proteins
-
physiological function
-
sortase A is involved in cell wall anchoring of pilus polymers
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-LPATG-diaminopropionic acid + H2O
2-aminobenzoyl-LPAT + G-diaminopropionic acid
show the reaction diagram
-
efficient cleavage
-
-
?
2-aminobenzoyl-LPETG-diaminopropionic acid +
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-LPETG-diaminopropionic acid + Gly5
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-LPETG-diaminopropionic acid + H2O
?
show the reaction diagram
-
evidence for a reverse protonation catalytic mechanism
-
-
?
2-aminobenzoyl-LPETG-diaminopropionic acid + H2O
2-aminobenzoyl-LPET + G-diaminopropionic acid
show the reaction diagram
-
cleavage between the threonine and the glycine residues, efficient cleavage
-
-
?
2-aminobenzoyl-LPNTA-diaminopropionic acid + H2O
2-aminobenzoyl-LPNT + A-diaminopropionic acid
show the reaction diagram
-
small amount of cleavage
-
-
?
4-([4-(dimethylamino)phenyl]-azo)-benzoyl-QALPETGEE-((2-aminoethyl)-amino)naphthalene-1-sulfonic acid + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
5(6)-carboxyfluorescein-6-aminohexanoic acid-LPKTGGRR-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
A33-LPETG-His6 + H2O
?
show the reaction diagram
-
A33 antigen extracellular domain bearing a His6 tag
-
-
?
Abz-KVENPQTNAGT-Dap(Dnp)-NH2 + GGGGG
?
show the reaction diagram
-
-
-
-
?
Abz-LPETG-Dap(Dnp)-NH2 + Gly-Gly-Gly-Gly-Gly
?
show the reaction diagram
-
-
-
-
?
Abz-LPETG-Dap(Dnp)-NH2 + Gly5
Abz-LPETGGGGG-OH + Gly-Dap(Dnp)-NH2
show the reaction diagram
-
-
-
-
?
Abz-LPETG-Dap(Dnp)-NH2 + Gly5
?
show the reaction diagram
-
transpeptidation of LPXTG-containing peptides to the cell-wall precursor mimic NH2-Ala2
-
-
?
Abz-LPETG-Dap(Dnp)-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-LPETGG-Dap(Dnp)-NH2 + Ala-Ala
Abz-LPETAA + GG-Dap(Dnp)-NH2
show the reaction diagram
Q99ZN4, -
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
show the reaction diagram
Streptococcus pyogenes SF370
Q99ZN4
transpeptidation of LPXTG-containing peptides to the cell-wall precursor mimic AlaAla
-
-
?
Abz-LPETGG-Dap(Dnp)-NH2 + GGGGG
?
show the reaction diagram
-
-
-
-
?
acetyl-ooocctcttacctcagttacaoooLPKTGGR-NH2 + H-GGGKLALKLALKALKAALKLA-NH2
acetyl-ooocctcttacctcagttacaoooLPKTGGGKLALKLALKALKAALKLA-NH2 + H-GGR-NH2
show the reaction diagram
-
-
-
-
?
agmatine + YALPETGK
(NH2)2-CN-(CH2)4-NH-(CO)-TEPLAY + ?
show the reaction diagram
-
transpeptidase reaction. The initially formed acyl-enzyme intermediate undergoes a hydrolysis followed by intra-molecular transpeptidation
-
-
?
AHLPKTGLR + 5-aminopentan-1-ol
?
show the reaction diagram
-
-
-
-
?
AHLPKTGLR + 6-aminohexyl 4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
?
show the reaction diagram
-
-
-
-
?
AHLPKTGLR + N-(2-(2-ethoxyethoxy)ethanamine)biotin amide
?
show the reaction diagram
-
-
-
-
?
AHLPKTGLR + N-hexylbiotin amide
?
show the reaction diagram
-
-
-
-
?
AHLPKTGLR-NH2 + triglycine
?
show the reaction diagram
-
-
-
-
?
aminobenzoyl-LPETG-diaminopropionic acid + GGGGG
aminobenzoyl-LPETGGGGG + G-diaminopropionic acid
show the reaction diagram
-
-
-
-
?
aminobenzoyl-LPETG-diaminopropionic acid + H2O
aminobenzoyl-LPET + G-diaminopropionic acid
show the reaction diagram
-
-
-
-
?
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2 + GGGGG
?
show the reaction diagram
-
-
-
-
?
aminobenzoyl-LPETG-dinitrophenyl ester + Gly-Gly-Gly
aminobenzoyl-LPETGGG + Gly-dinitrophenyl ester
show the reaction diagram
-
HPLC results provide direct evidence for the formation of the kinetically competent acyl enzyme intermediate
-
-
?
Dabcyl-LPETG-Edans + H2O
Dabcyl-LPET + Gly-Edans
show the reaction diagram
-
-
-
-
?
Dabcyl-SFLPKTGM-Edans + H2O
?
show the reaction diagram
Staphylococcus aureus, Staphylococcus aureus 515
-
the substrate mimicks the LPXTG motif of pilus 2a minor ancillary protein
-
-
?
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-2,4-dinitrophenol + Gly-Gly-Gly
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-Gly-Gly + Gly-2,4-dinitrophenol
show the reaction diagram
-
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-dinitrophenol + H2O
o-aminobenzoyl-Leu-Pro-Glu-Thr + Gly-2,4-dinitrophenol
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-LPETG-2,4-dinitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
PrtP protein + H2O
?
show the reaction diagram
Lactococcus lactis, Lactococcus lactis IL1403
-
-
-
-
?
recombinant Helicobacter pylori R1,3-fucosyltransferase + triglycine
?
show the reaction diagram
-
-
-
-
?
recombinant human beta1,4-galactosyltransferase + N-(2-(2-ethoxyethoxy)ethanamine)biotin amide
?
show the reaction diagram
-
-
-
-
?
recombinant human beta1,4-galactosyltransferase + N-hexylbiotin amide
?
show the reaction diagram
-
-
-
-
?
YALPETGK + H2O
YALPET + Gly-Lys
show the reaction diagram
-
-
-
-
?
YbeF protein + H2O
?
show the reaction diagram
Lactococcus lactis, Lactococcus lactis IL1403
-
-
-
-
?
YhgE protein + H2O
?
show the reaction diagram
Lactococcus lactis, Lactococcus lactis IL1403
-
-
-
-
?
YndF protein + H2O
?
show the reaction diagram
Lactococcus lactis, Lactococcus lactis IL1403
-
-
-
-
?
YwfG protein + H2O
?
show the reaction diagram
Lactococcus lactis, Lactococcus lactis IL1403
-
-
-
-
?
[4-(4-dimethylaminophenylazo)benzoic acid]-QALPETGEE-[5-[2'-(aminoethyl)amino]-naphthalenesulfonic acid] + H2O
?
show the reaction diagram
-
-
-
-
?
Dnp-AQALPETGEE-NH2 + Gly5
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
Q9S446
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
?
-
-
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, 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
?
-
Q9S446
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
?
-
-
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
?
-
-
the transpeptidase required for cell wall protein anchoring and virulence in Staphylococcus aureus
-
-
-
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
?
-
-
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
?
-
-
sortase A may be critical in the early stage of inhaltation anthrax
-
-
-
additional information
?
-
-
sortase A plays a role in the establishment of infections
-
-
-
additional information
?
-
-
no cleavage of 2-aminobenzoyl-NPKTG-diaminopropionic acid and 2-aminobenzoyl-LGATG-diaminopropionic acid
-
-
-
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
?
-
-
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 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
?
-
-
sortase localization is facilitated by a positive charge that is necessary for efficient pilus biogenesis
-
-
-
additional information
?
-
-
SrtA is dispensable for pilus assembly and localization to the cell wall
-
-
-
additional information
?
-
-
SrtA is involved in the virulence manifestation of streptococcal toxic shock syndrome
-
-
-
additional information
?
-
B9DS55
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
-
-
-
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
?
-
-
SrtA recognizes the LPXTG-sorting signal through a lock-in-key mechanism
-
-
-
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, 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
?
-
Staphylococcus aureus 515
-
no activity with Dabcyl-KGIIPKTGGK-Edans, Dabcyl-KKVTIPQTGGIGT-Edans and Dabcyl-SFIPKTGM-Edans, truncated SrtADELTAN40 also catalyzes in vitro transpeptidation reaction
-
-
-
additional information
?
-
Staphylococcus aureus Newman
-
sortase A plays a role in the establishment of infections
-
-
-
additional information
?
-
Corynebacterium diphtheriae NCTC13129
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
?
-
Q9S446
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
?
-
-
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
?
-
-
the transpeptidase required for cell wall protein anchoring and virulence in Staphylococcus aureus
-
-
-
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
?
-
-
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
?
-
-
sortase localization is facilitated by a positive charge that is necessary for efficient pilus biogenesis
-
-
-
additional information
?
-
-
SrtA is dispensable for pilus assembly and localization to the cell wall
-
-
-
additional information
?
-
-
SrtA is involved in the virulence manifestation of streptococcal toxic shock syndrome
-
-
-
additional information
?
-
Corynebacterium diphtheriae NCTC13129
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
2 mM, 8fold stimulation of activity, binding near the active site stimulates catalysis possibly by altering the conformation of a surface loop that recognizes newly translocated polypeptides
Ca2+
-
a single Ca2+ bound to an ordered pocket on SrtA allosterically activates catalysis by modulating both the structure and dynamics of a large active site loop
Mg2+
-
can substitute in part for Ca2+
Mn2+
-
can substitute in part for Ca2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1E)-N'-[(1E)-(4-[(E)-[(diaminomethylene)hydrazono]methyl]phenyl)methylene]ethanehydrazonamide
-
-
(2-(trimethylammonium)ethyl)methanethiosulfonate
-
inibition 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-(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-(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-(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
-
-
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
berberine chloride
-
potential of this inhibitor for the treatment of Staphylococcus aureus infections
berberine chloride
-
-
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
bis(4-ethoxy-2-phenyl-5-pyridazyl)disulfide
-
-
cis-1,2-bis(phenylsulfonyl)ethylene
-
IC50: 0.00113 mM, irreversible
demethylaaptamine
-
-
demethyloxyaaptamine
-
-
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
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
kaempferol
-
IC50 for recombinant SrtA(DELTA24): 0.07794 mM, no antibacterial activity against Staphylococcus aureus
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 2-morpholin-4-yl-5-[[(2E)-3-(2-thienyl)prop-2-enoyl]amino]benzoate
-
-
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
-
-
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
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
-
-
phenyl vinyl sulfone
-
IC50: 0.736 mM, irreversible
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
methyl vinyl sulfone
-
IC50: 0.00624 mM, irreversible
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00824
-
2-aminobenzoyl-LPETG-diaminopropionic acid
-
37C, pH 7.5, wild-type enzyme
0.00932
-
2-aminobenzoyl-LPETG-diaminopropionic acid
-
37C, pH 7.5, mutant enzyme N98Q
0.0097
-
2-aminobenzoyl-LPETG-diaminopropionic acid
-
37C, pH 7.5, mutant enzyme N98A
0.01391
-
2-aminobenzoyl-LPETG-diaminopropionic acid
-
37C, pH 7.5, mutant enzyme R197K
0.01597
-
2-aminobenzoyl-LPETG-diaminopropionic acid
-
37C, pH 7.5, mutant enzyme R197A
0.0168
-
2-aminobenzoyl-LPETG-diaminopropionic acid
-
37C, pH 7.5, mutant enzyme R197H
5.5
-
Abz-LPETG-Dap(Dnp)-NH2
-
37C, pH 7.5
5.5
-
Abz-LPETG-Dap(Dnp)-NH2
-
-
1.18
-
agmatine
-
at 37C, pH not specified in the publication, transpeptidation reaction
0.79
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
mutant enzyme
3.8
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
mutant enzyme
4.7
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
mutant enzyme
6.7
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
mutant enzyme
8.5
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
mutant enzyme
10.6
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
wild-type enzyme
11.2
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
mutant enzyme
4.69
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme R197A
6.56
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme V168A
6.74
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme E171A
8.13
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme D170A
8.7
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme G167A
8.76
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, wild-type enzyme
9.14
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme L169A
10.4
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme R197K
12.7
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme Q172A
13.7
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme R197Cit
5.6
-
Dnp-AQALPETGEE-NH2
-
-
0.041
-
Gly-Gly-Gly
-
pH 7.5, transpeptidation with o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-2,4-dinitrophenol
0.2
-
Gly-Gly-Gly
-
-
0.02
-
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-2,4-dinitrophenol
-
hydrolysis reaction
0.117
-
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-2,4-dinitrophenol
-
pH 7.5, transpeptidation with Gly-Gly-Gly
0.035
-
o-aminobenzoyl-LPETG-2,4-dinitrophenyl
-
sortase A DELTA64 (residues Asp65Lys210), in 20 mM HEPES, pH 7.5
0.038
-
o-aminobenzoyl-LPETG-2,4-dinitrophenyl
-
sortase A DELTA56 (residues Asp-57-Lys210), in 20 mM HEPES, pH 7.5
0.00013
-
o-aminobenzoyl-LPETG-2,4-dinitrophenyl ester
-
mutant enzyme E108A
0.0018
-
o-aminobenzoyl-LPETG-2,4-dinitrophenyl ester
-
mutant enzyme E171A
0.0085
-
o-aminobenzoyl-LPETG-2,4-dinitrophenyl ester
-
wild-type enzyme
0.0087
-
o-aminobenzoyl-LPETG-2,4-dinitrophenyl ester
-
mutant enzyme D170A
1.59
-
YALPETGK
-
at 37C, pH not specified in the publication
-
0.14
-
Gly5
-
37C, pH 7.5
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00019
-
2-aminobenzoyl-LPETG-diaminopropionic acid
-
37C, pH 7.5, mutant enzyme R197K
0.00021
-
2-aminobenzoyl-LPETG-diaminopropionic acid
-
37C, pH 7.5, mutant enzyme R197A
0.00098
-
2-aminobenzoyl-LPETG-diaminopropionic acid
-
37C, pH 7.5, mutant enzyme R197H
0.29
-
2-aminobenzoyl-LPETG-diaminopropionic acid
-
37C, pH 7.5, mutant enzyme N98A
0.3
-
2-aminobenzoyl-LPETG-diaminopropionic acid
-
37C, pH 7.5, wild-type enzyme
0.37
-
2-aminobenzoyl-LPETG-diaminopropionic acid
-
37C, pH 7.5, mutant enzyme N98Q
0.27
-
Abz-LPETG-Dap(Dnp)-NH2
-
37C, pH 7.5
0.27
-
Abz-LPETG-Dap(Dnp)-NH2
-
-
0.000019
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
mutant enzyme
0.0003
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
mutant enzyme
0.00046
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
mutant enzyme
0.0006
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
mutant enzyme
0.69
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
wild-type enzyme
0.72
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
mutant enzyme
0.78
-
aminobenzoyl-LPETG-diaminopropionyl(dinitrophenyl)-NH2
-
mutant enzyme
0.000628
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme R197A
0.0019
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme R197K
0.0123
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme L169A
0.15
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme V168A
0.16
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme E171A
0.29
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme R197Cit
1.09
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme D170A
1.1
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, wild-type enzyme
1.13
-
aminobenzoyl-LPETGG-diaminopropionic acid(dinitrophenol)-NH2
-
37C, pH 7.5, mutant enzyme G167A; 37C, pH 7.5, mutant enzyme Q172A
0.013
-
Dnp-AQALPETGEE-NH2
-
-
0.0000067
-
o-aminobenzoyl-LPETG-2,4-dinitrophenyl
-
sortase A DELTA56 (residues Asp-57-Lys210), in 20 mM HEPES, pH 7.5
0.0000083
-
o-aminobenzoyl-LPETG-2,4-dinitrophenyl
-
sortase A DELTA64 (residues Asp65Lys210), in 20 mM HEPES, pH 7.5
0.18
-
Gly-Gly-Gly
-
-
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000183
-
o-aminobenzoyl-LPETG-2,4-dinitrophenyl
-
sortase A DELTA56 (residues Asp-57-Lys210), in 20 mM HEPES, pH 7.5
302626
0.000233
-
o-aminobenzoyl-LPETG-2,4-dinitrophenyl
-
sortase A DELTA64 (residues Asp65Lys210), in 20 mM HEPES, pH 7.5
302626
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00003
-
4-ethoxy-5-(2-pyridyldithio)-2-phenylpyridazin-3-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.0004
-
4-ethoxy-5-(methyldithio)-2-phenylpyridazin-3-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.00000021
-
benzyloxycarbonyl-Leu-Pro-Ala-Thr-CH2Cl
-
pH 7.5, 37C
0.00000022
-
benzyloxycarbonyl-Leu-Pro-Ala-Thr-CHN2
-
pH 7.5, 37C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.275
-
(1E)-N'-[(1E)-(4-[(E)-[(diaminomethylene)hydrazono]methyl]phenyl)methylene]ethanehydrazonamide
-
-
0.133
-
(2-methyl-1H-indol-3-yl)(oxo)acetic acid
-
pH and temperature not specified in the publication
0.476
-
(2E)-2,3-bis(4-methoxyphenyl)acrylamide
-
IC50: 0.476 mM
0.187
-
(2E)-2,3-bis(4-methoxyphenyl)acrylonitrile
-
IC50: 0.187 mM
0.15
-
(2E)-2-(2-furoyl)-3-[(methyl[4-[(5-nitropyridin-2-yl)oxy]phenyl]oxido-l4-sulfanylidene)amino]acrylonitrile
-
-
0.111
-
(2E)-3-(2-furyl)-N-[3-(hydroxymethyl)-4-morpholin-4-ylphenyl]acrylamide
-
-
0.4
-
(2E)-3-[(methyl[4-[(5-nitropyridin-2-yl)oxy]phenyl]oxido-l4-sulfanylidene)amino]-2-(2-thienylcarbonyl)acrylonitrile
-
-
0.125
-
(2E)-4-([4-[(2-hydroxybenzoyl)amino]phenyl]amino)-4-oxobut-2-enoic acid
-
-
0.107
-
(2E)-N-(3-formyl-4-morpholin-4-ylphenyl)-3-(2-furyl)acrylamide
-
-
0.077
-
(2E)-N-(3-formyl-4-morpholin-4-ylphenyl)-3-(2-thienyl)acrylamide
-
-
0.073
-
(2E)-N-[3-(hydroxymethyl)-4-morpholin-4-ylphenyl]-3-(2-thienyl)acrylamide
-
-
0.0279
-
(2Z)-2,3-bis(4-methoxyphenyl)acrylonitrile
-
IC50: 0.0279mM
0.009244
-
(2Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
-
IC50: 0.009244 mM
0.0362
-
(2Z)-3-(2-methoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
-
IC50: 0.0362 mM
0.02296
-
(2Z)-3-(3,4-dimethoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
-
IC50: 0.02296 mM
0.025463
-
(2Z)-3-(3,5-dimethoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
-
IC50: 0.025463 mM
0.0174
-
(2Z)-3-(3-methoxyphenyl)-2-(4-methoxyphenyl)acrylonitrile
-
IC50: 0.0174 mM
0.0052
-
(4E)-5-methyl-4-[[(4-nitrophenyl)amino]methylidene]-2-phenyl-2,4-dihydro-3H-pyrazole-3-thione
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.119
-
(5Z)-3-(2,4-dimethylphenyl)-5-(3-nitrobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
1
-
(5Z)-3-(3-chlorophenyl)-5-(4-methyl-3-nitrobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
IC50 above 1.0 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.492
-
(5Z)-3-benzyl-5-benzylidene-2-thioxo-1,3-thiazolidin-4-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.104
-
(5Z)-3-ethyl-5-(2-nitrobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.0037
-
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-(2,4-dimethylphenyl)-2-thioxo-1,3-thiazolidin-4-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.017
-
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-(3-chlorophenyl)-2-thioxo-1,3-thiazolidin-4-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.015
-
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-(3-methylphenyl)-2-thioxo-1,3-thiazolidin-4-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.012
-
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-(4-nitrophenyl)-2-thioxo-1,3-thiazolidin-4-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.014
-
(5Z)-5-(3-bromo-2-hydroxy-5-nitrobenzylidene)-3-phenyl-2-thioxo-1,3-thiazolidin-4-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.035
-
(5Z)-5-(3-bromo-4-hydroxy-5-nitrobenzylidene)-3-(2,4-dimethylphenyl)-2-thioxo-1,3-thiazolidin-4-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.109
-
(5Z)-5-(3-chlorobenzylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.199
-
(5Z)-5-benzylidene-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.405
-
(5Z)-5-benzylidene-3-methyl-2-thioxo-1,3-thiazolidin-4-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.186
-
(5Z)-5-benzylidene-3-propyl-2-thioxo-1,3-thiazolidin-4-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.0896
-
1-(3,4-dichlorophenyl)-3-(dimethylamino)propan-1-one
-
-
0.0904
-
1-(3,4-dichlorophenyl)-3-(dimethylamino)propan-1-one
-
-
0.0569
-
1-(4-bromophenyl)-3-(3-methylpiperidin-1-yl)propan-1-one
-
-
0.0837
-
1-(4-bromophenyl)-3-(3-methylpiperidin-1-yl)propan-1-one
-
-
0.0844
-
1-(4-chlorophenyl)-3-morpholin-4-ylpropan-1-one
-
-
0.0906
-
1-(4-chlorophenyl)-3-morpholin-4-ylpropan-1-one
-
-
0.0472
-
1-(4-fluorophenyl)-3-morpholin-4-ylpropan-1-one
-
-
0.0891
-
1-(4-fluorophenyl)-3-morpholin-4-ylpropan-1-one
-
-
0.0569
-
1-(4-methylphenyl)-3-morpholin-4-ylpropan-1-one
-
-
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
-
pH and temperature not specified in the publication
0.097
-
1-phenyl-4,9-dihydro-3H-beta-carboline
-
pH and temperature not specified in the publication
0.4
-
1-[4-(2-aminopyrimidin-4-yl)phenyl]-3-(4-chlorophenyl)urea
-
-
0.069
-
1H-indol-3-yl(oxo)acetic acid
-
pH and temperature not specified in the publication
0.174
-
2-(1H-indol-3-yl)-2-oxo-N-phenylacetamide
-
pH and temperature not specified in the publication
0.061
-
2-(2-methyl-1H-indol-3-yl)-2-oxo-N-phenylacetamide
-
pH and temperature not specified in the publication
0.301
-
2-(3,5-dichlorophenyl)-4-(ethylsulfanyl)-5-sulfanylpyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.166
-
2-(3,5-dichlorophenyl)-5-ethoxy-4-sulfanylpyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
2-(3-bromophenyl)-4,5-dichloropyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
2-(3-bromophenyl)-4-(ethylsulfanyl)-5-sulfanylpyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
2-(3-bromophenyl)-4-chloro-5-ethoxypyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
2-(3-bromophenyl)-5-chloro-4-ethoxypyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
2-(3-bromophenyl)-5-chloro-4-methoxypyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.0045
-
2-(3-chlorophenyl)-4-methoxy-5-sulfanylpyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
2-(4-nitrophenyl)-4,5-dichloropyridazin-3-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.0179
-
2-cyclohexyl-4-(ethylsulfanyl)-5-sulfanylpyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
2-ethyl-4-hydroxy-5-(methylsulfanyl)pyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.226
-
2-hydroxy-N-[4-[([[(4-methylphenyl)sulfonyl]amino]carbonyl)amino]phenyl]benzamide
-
-
0.105
-
2-morpholin-4-yl-5-[[(2E)-3-(2-thienyl)prop-2-enoyl]amino]benzamide
-
-
0.05
-
2-phenyl-4,5-dichloro-pyridazin-3-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.19
-
3,3,3-trifluoro-1-(phenylsulfonyl)-1-propene
-
IC50: 0.19 mM, irreversible
0.0973
-
3,5-bis[[2-(4-nitrophenyl)-2-oxoethyl]thio]isothiazole-4-carbonitrile
-
-
0.0548
-
3-(dimethylamino)-1-(2-thienyl)propan-1-one
-
-
0.0907
-
3-(dimethylamino)-1-(2-thienyl)propan-1-one
-
-
0.0543
-
3-(dimethylamino)-1-(3-nitrophenyl)propan-1-one
-
-
0.0902
-
3-(dimethylamino)-1-(3-nitrophenyl)propan-1-one
-
-
0.066
-
3-anilino-1-(3-nitrophenyl)propan-1-one
-
-
0.0873
-
3-anilino-1-(3-nitrophenyl)propan-1-one
-
-
0.061
-
4,5-dichloro-2-(3,5-dichlorophenyl)pyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
4,5-dichloro-2-(3-fluorophenyl)pyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
4,5-dichloro-2-(3-methylphenyl)pyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
4,5-dichloro-2-cyclohexylpyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
4-(benzyloxy)-5-hydroxy-2-phenylpyridazin-3(2H)-one
-
IC50 above 0.05 mM,
0.0055
-
4-(ethylsulfanyl)-2-(3-fluorophenyl)-5-sulfanylpyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.0033
-
4-(ethylsulfanyl)-2-(3-methylphenyl)-5-sulfanylpyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.03
-
4-(ethylsulfanyl)-2-(4-nitrophenyl)-5-sulfanylpyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.0014
-
4-(ethylsulfanyl)-2-phenyl-5-sulfanylpyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
4-(ethylsulfanyl)-5-hydroxy-2-phenylpyridazin-3(2H)-one
-
IC50 above 0.05 mM,
0.05
-
4-chloro-2-(3,5-dichlorophenyl)-5-ethoxypyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
4-chloro-2-cyclohexyl-5-ethoxypyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
4-chloro-5-(methylsulfanyl)-2-phenylpyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
4-chloro-5-ethoxy-2-(3-fluorophenyl)pyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
4-chloro-5-ethoxy-2-(3-methylphenyl)pyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.219
-
4-chloro-5-ethoxy-2-(4-nitrophenyl)pyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.001
-
4-chloro-5-ethoxy-2-phenylpyridazin-3-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.0002
-
4-ethoxy-2-phenyl-5-sulfanylpyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.013
-
4-ethoxy-5-mercapto-2-phenylpyridazin-3-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
4-hydroxy-5-(methylsulfanyl)-2-phenylpyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
5-chloro-2-(3,5-dichlorophenyl)-4-ethoxypyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
5-chloro-2-(3,5-dichlorophenyl)-4-methoxypyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
5-chloro-2-(3-fluorophenyl)-4-methoxypyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
5-chloro-2-cyclohexyl-4-ethoxypyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
5-chloro-2-cyclohexyl-4-methoxypyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
5-chloro-4-ethoxy-2-(3-fluorophenyl)pyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
5-chloro-4-ethoxy-2-(3-methylphenyl)pyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
5-chloro-4-ethoxy-2-(4-nitrophenyl)pyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
5-chloro-4-ethoxy-2-phenylpyridazin-3-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
5-chloro-4-methoxy-2-(3-methylphenyl)pyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
5-chloro-4-methoxy-2-phenylpyridazin-3(2H)-one
-
IC50 above 0.05 mM, in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.0057
-
5-ethoxy-2-(3-fluorophenyl)-4-sulfanylpyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.0031
-
5-ethoxy-2-(3-methylphenyl)-4-sulfanylpyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.0044
-
5-ethoxy-2-phenyl-4-sulfanylpyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.05
-
5-hydroxy-4-methoxy-2-phenylpyridazin-3(2H)-one
-
IC50 above 0.05 mM,
0.0093
-
5-methoxy-2-phenyl-4-sulfanylpyridazin-3(2H)-one
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.181
-
5-[[(2E)-3-(2-furyl)prop-2-enoyl]amino]-2-morpholin-4-ylbenzoic acid
-
-
0.067
-
6-hydroxydihydro-beta-carboline
-
pH and temperature not specified in the publication
-
0.0115
-
7-methoxy-1-phenyl-2,3,4,9-tetrahydro-1H-beta-carboline
-
pH and temperature not specified in the publication
0.025
-
7-methoxy-1-phenyl-4,9-dihydro-3H-beta-carboline
-
pH and temperature not specified in the publication
0.0015
-
bis(4-ethoxy-2-phenyl-5-pyridazyl)disulfide
-
in 20 mM HEPES, 5 mM CaCl2, 0.05% (v/v) Tween-20, pH 7.5, at 25C
0.00113
-
cis-1,2-bis(phenylsulfonyl)ethylene
-
IC50: 0.00113 mM, irreversible
0.00106
-
divinyl sulfone
-
IC50: 0.00106 mM, irreversible
0.0802
-
ethyl 4-[3-(4-bromophenyl)-3-oxopropyl]piperazine-1-carboxylate
-
-
0.0907
-
ethyl 4-[3-(4-bromophenyl)-3-oxopropyl]piperazine-1-carboxylate
-
-
0.00471
-
ethyl vinyl sulfone
-
IC50: 0.00471 mM, irreversible
0.123
-
galangin
-
IC50 for recombinant SrtA(DELTA24): 0.123 mM, no antibacterial activity against Staphylococcus aureus
0.1179
-
galangin-3-methyl ether
-
IC50 for recombinant SrtA(DELTA24): 0.1179 mM, no antibacterial activity against Staphylococcus aureus
0.05886
-
isorhamnetin
-
IC50 for recombinant SrtA(DELTA24): 0.05886 mM, no antibacterial activity against Staphylococcus aureus
0.07794
-
kaempferol
-
IC50 for recombinant SrtA(DELTA24): 0.07794 mM, no antibacterial activity against Staphylococcus aureus
0.231
-
methyl (2E)-2,3-bis(4-methoxyphenyl)acrylate
-
IC50: 0.231 mM
2.2
-
methyl (2S,3S,7aS)-2-ethenesulfonyl-5-oxo-3-phenyltetrahydropyrrolizine-7a-carboxylate
-
pH 7.5, 37C
2.47
-
methyl (2S,3S,7aS)-2-ethenesulfonyl-5-oxo-3-pyridin-3-yl-tetrahydropyrrolizine-7a-carboxylate
-
pH 7.5, 37C
2.68
-
methyl (2S,3S,7aS)-3-(3,4-dimethoxyphenyl)-2-ethenesulfonyl-5-oxotetrahydropyrrolizine-7a-carboxylate
-
pH 7.5, 37C
1.86
-
methyl (2S,4S,5S)-4-ethenesulfonyl-2-(2-methoxycarbonylethyl)-5-pyridin-3-yl-pyrrolidine-2-carboxylate
-
pH 7.5, 37C
0.909
-
methyl (2Z)-2,3-bis(4-methoxyphenyl)acrylate
-
IC50: 0.909 mM
1.32
-
methyl (4S,5S)-4-(ethenylsulfonyl)-5-(2-fluorophenyl)-L-prolinate
-
pH 7.5, 37C
1.04
-
methyl (4S,5S)-4-(ethenylsulfonyl)-5-(3-fluorophenyl)-L-prolinate
-
pH 7.5, 37C
0.85
-
methyl (4S,5S)-4-(ethenylsulfonyl)-5-phenyl-L-prolinate
-
pH 7.5, 37C
0.071
-
methyl 2-morpholin-4-yl-5-[[(2E)-3-(2-thienyl)prop-2-enoyl]amino]benzoate
-
-
0.0698
-
methyl 4-[3-(dimethylamino)propanoyl]benzenesulfinate
-
-
0.0913
-
methyl 4-[3-(dimethylamino)propanoyl]benzenesulfinate
-
-
0.058
-
methyl 5-[[(2E)-3-(2-furyl)prop-2-enoyl]amino]-2-morpholin-4-ylbenzoate
-
-
0.03739
-
morin
-
IC50 for recombinant SrtA(DELTA24): 0.03739 mM, no antibacterial activity against Staphylococcus aureus
0.04403
-
myricetin
-
IC50 for recombinant SrtA(DELTA24): 0.04403 mM, no antibacterial activity against Staphylococcus aureus
0.042
-
p-hydroxymercuribenzoic acid
-
pH and temperature not specified in the publication
0.736
-
phenyl vinyl sulfone
-
IC50: 0.736 mM, irreversible
0.0527
-
quercetin
-
IC50 for recombinant SrtA(DELTA24): 0.0527 mM, no antibacterial activity against Staphylococcus aureus
0.05361
-
quercetin-3,3'-dimethyl ether
-
IC50 for recombinant SrtA(DELTA24): 0.05361 mM, no antibacterial activity against Staphylococcus aureus
0.00624
-
methyl vinyl sulfone
-
IC50: 0.00624 mM, irreversible
additional information
-
additional information
-
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
-
kidney of Mus musculus infected with Staphylococcus aureus. mRNA levels of sortase A decrease over time, from day 3 of infection to day 14. The transcript number of srtA decreases faster in septic mice than in mice with a non-septic disease
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
class A sortases adopt a type II membrane topology (N terminus inside and C terminus outside the cytoplasm), class B enzymes represent type I membrane proteins (N terminus outside, C terminus inside)
Manually annotated by BRENDA team
-
sortase A (SrtA) colocalizes with SecA at single foci in the enterococcus. Proteins that localize to single foci in Enterococcus faecalis share a positively charged domain flanking a transmembrane helix. Positively charged domain can act as a localization retention signal for the focal compartmentalization of the membrane protein
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
17800
-
-
SDS-PAGE
23000
-
-
SDS-PAGE, immune-reactive species
additional information
-
-
signal peptide, membrane anchor and a shorter linker domain of sortase enzymes display no amino acid conservation. The core residue, SrtA residues 60-206, is present in all sortase homologs examined, suggesting that this domain may comprise the catalytically active domain
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 16595, SrtDELTAN59, electrospray ionization mass spectrometry
?
-
x * 27000, SDS-PAGE
?
-
x * 23900, truncated enzyme, calculated from amino acid sequence; x * 25000, truncated enzyme, SDS-PAGE
?
Staphylococcus aureus 515
-
x * 23900, truncated enzyme, calculated from amino acid sequence; x * 25000, truncated enzyme, SDS-PAGE
-
dimer
-
the dimeric form of SrtA is more active than the monomeric enzyme
monomer
-
the dimeric form of SrtA is more active than the monomeric enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystals are grown by the hanging-drop technique with a protein concentration of 50 mg/ml in 25 mM MES buffer, pH 6.35. The crystallization conditions include 3.2 M ammonium sulfate, 0.1 M NaCl, and trace amounts of ethylene glycol. Crystal structure of native SrtA, of an active-site mutant of SrtA, and of the mutant SrtA complexed with its substrate LPETG peptide
-
hanging drop method of vapor diffusion at 20C, SrtA residues Val82-Thr249 (catalytic domain)
Q99ZN4, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by Ni-NTA affinity chromatography
-
Talon His-affinity resin column chromatography and Sephacryl-100 gel filtration
-
HisTrapHP column chromatography, gel filtration
-
HiTrap Chelating HP column chromatography and Superdex 75 gel filtration
-
N-terminally His6-tagged SrtADELTAN24 expressed in Escherichia coli BL21
-
Ni-NTA column chromatography
-
Ni2+-HisTrap column chromatography
-
of SrtADELTAN59 and mutant proteins
-
purification of SrtADELTAN59 and SrtA wild-type proteins
-
recombinant sortase A-GST fusion protein
-
recombinant SrtA lacking the amino-terminal 24 amino acids
-
recombinant SrtADELTAN24 in a His6-tagged form
-
Talon resin column chromatography
-
recombinant enzyme, SrtA residues Val82-Thr249 (catalytic domain)
Q99ZN4, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloned into the plasmid vector pQE30
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression of SrtADELTAN24 in a His6-tagged form
-
mutant enzymes expressed in Escherichia coli
-
N-terminally His6-tagged SrtA lacking the amino-terminal 24 amino acids is expressed in BL21(DE3) cells containing the plasmid pET15bSrtADN24
-
N-terminally His6-tagged SrtADELTAN24 is expressed in Escherichia coli BL21
-
overexpression in Escherichia coli
-
recombinant mature sortase A (without the N-terminal signal peptide) is produced as GST fusion in Escherichia coli
-
SrtADELTA24 is expressed in Escherichia coli
-
wild-type and variant SrtA proteins
-
expressed in Escherichia coli BL21 cells
-
DNA sequence encoding SrtA residues Val82-Thr249, expression in Escherichia coli BL21
Q99ZN4, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C184A
-
mutant enzyme can not cleave the LPXTG motif
C184A
-
catalytically inactive
C184S
-
2700fold decrease in kcat/Km compared to wild-type value
D170A
-
turnover-number for o-aminobenzoyl-LPETG-2,4-dinitrophenyl is nearly identical to wild-type value
D170A
-
Tm is 1.7C higher than the Tm-value of wild-type enzyme. No change in kcat/Km compared to wild-type value
D185A 1.3
-
fold decrease in kcat/Km compared to wild-type value
D186A
-
1.8fold decrease in kcat/Km compared to wild-type value
DELTA N59
-
trucation of N-terminal 59 amino acids does not affect the activity of the enzyme
DELTA N59
-
enhanced solubility of the mutant helps the crystallization; trucation of N-terminal 59 amino acids does not affect the activity of the enzyme
E108A
-
turnover-number for o-aminobenzoyl-LPETG-2,4-dinitrophenyl is 43.8fold lower than wild-type value
E171A
-
turnover-number for o-aminobenzoyl-LPETG-2,4-dinitrophenyl is 4.7fold lower than wild-type value
E171A
-
Tm is 1.8C lower than the Tm-value of wild-type enzyme. kcat/Km is 5.4fold lower than wild-type value
G167A
-
Tm is 0.5C lower than the Tm-value of wild-type enzyme. No change in kcat/KM compared to wild-type enzyme
H120A
-
96000fold decrease in kcat/Km compared to wild-type value
H120Q
-
36000fold decrease in kcat/Km compared to wild-type value
I123G
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template. Mutation reduces dimerization
I182A
-
mutation produces modest decreases in SrtA activity and leds to substrate inhibition. 28fold decrease in kcat/Km compared to wild-type value
I182S
-
74fold decrease in kcat/Km compared to wild-type value
K137A
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template. Mutation completely disrupts dimerization
K152A
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template. Mutation increases dimerization
K62A
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template
L169A
-
Tm is 1.8C lower than the Tm-value of wild-type enzyme. kcat/Km is 93fold lower than wild-type value
N132A
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template. Mutation completely disrupts dimerization
N98A
-
kcat/Km is 1.2fold lower than wild-type value
N98Q
-
kcat/Km is 1.1fold higher than wild-type value
P126G
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template. Mutation reduces dimerization
Q172A
-
Tm is 1.2C lower than the Tm-value of wild-type enzyme. kcat/Km is 1.4fold lower than wild-type value
R197A
-
kcat/Km is 2769fold lower than wild-type value
R197A
-
540fold decrease in kcat/Km compared to wild-type value
R197A
-
Tm is 2.9C lower than the Tm-value of wild-type enzyme. kcat/Km is 960fold lower than wild-type value
R197Cit
-
generation of a semi-synthetic SrtA in which Arg197 is replaced with citrulline, a nonionizable analog. This change results in less than a 3fold decrease in kcat/KM, indicating that Arg197 utilizes a hydrogen bond, rather than an electrostatic interaction. Tm is 0.3C higher than the Tm-value of wild-type enzyme; kcat/Km is 5.9fold lower than wild-type value
R197H
-
kcat/Km is 610fold lower than wild-type value
R197K
-
kcat/Km is 2571fold lower than wild-type value
R197K
-
1000fold decrease in kcat/Km compared to wild-type value
R197K
-
Tm is 2C lower than the Tm-value of wild-type enzyme. kcat/Km is 690fold lower than wild-type value
T180A
-
mutation produces modest decreases in SrtA activity and leds to substrate inhibition. 14fold decrease in kcat/Km compared to wild-type value
T183A
-
1200fold decrease in kcat/Km compared to wild-type value
V168A
-
Tm is 1.7C lower than the Tm-value of wild-type enzyme. kcat/Km is 5.5fold lower than wild-type value
H126A
-
inactive
additional information
-
srtA mutants AHG263 (srtA gene deleted by allelic replacement with ermC marker) and AHG188
L181A
-
mutation produces modest decreases in SrtA activity and leds to substrate inhibition. 7.6fold decrease in kcat/Km compared to wild-type value
additional information
-
marked changes in the specificity profile of SrtA are obtained by replacing the beta6/beta7 loop in SrtA with the corresponding domain from SrtB. The chimeric beta6/beta7 loop swap enzyme (SrtLS) conferrs the ability to acylate NPQTN-containing substrates, with a kcat/Kmapp of 0.0062 /M * s. This enzyme is unable to perform the transpeptidation stage of the reaction, suggesting that additional domains are required for transpeptidation to occur. The overall catalytic specificity profile (kcat/Kmapp (NPQTN)/kcat/Kmapp (LPETG)) of SrtLS is altered 700000fold from SrtA. These results indicate that the beta6/beta7 loop is an important site for substrate recognition in sortases
additional information
-
the F40-sortase mutant loses activity compared to the wild type enzyme and prefers ligation of the FPxTG motif over the native LPxTG sequence. The F40-sortase possesses a remarkable broad selectivity and accepted aromatic amino acids as well as residues with small side chains, including Ala, Asp, Ser, Pro, and Gly, at position 1 of the sorting motif
Y143A
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template. Mutation completely disrupts dimerization
additional information
-
srtA-deficient mutant, colonizes the nasopharynx at a significantly lower level than the D39 parent strain during the second and third week of the carriage, and was eliminated from the nasopharynx one week earlier than the D39 pneumococci
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
Bacillus anthracis SrtA anchors surface proteins bearing LPXTG motif sorting signals to the cell wall envelope of vegetative bacilli, srtA gene of Bacillus anthracis is not required for the development of acute anthrax disease in A/J mice
analysis
-
development of a reverse-phase HPLC assay to identify and characterize sortase reaction intermediates
medicine
Q9S446
in principle the purified SrtA protein can be used to screen for compounds that inhibit cell wall sorting, a strategy that may lead to new therapies for human infections caused by Gram-positive bacteria
medicine
-
substrate-derived irreversible inhibitors of SrtA that might find application in delineating the role of the cysteine protease-transpeptidase in cell surface protein sorting and adherence of Gram-positive organisms
medicine
-
potential of inhibitors for the treatment of Staphylococcus aureus infections: (Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl) acrylonitrile, beta-sitosterol-3-O-glucopyranoside, berberine chloride and psammaplin A1
medicine
-
SrtA activity is a prime target for inhibition of Staphylococcus aureus colonization
medicine
-
4-vinylsulfonyl 5-phenyl prolinates inhibit Staphylococcus aureus sortase SrtA irreversibly by modification of the enzyme Cys184 and could be used as hits for the development of antibacterials and antivirulence agents
molecular biology
-
a general strategy for the site-specific modification of cell surface proteins with synthetic molecules by using sortase, a transpeptidase from Staphylococcus aureus. The short peptide tag LPETGG is genetically introduced to the C terminus of the target protein, expressed on the cell surface. Subsequent addition of sortase and an N-terminal triglycine-containing probe results in the site-specific labeling of the tagged protein. C-terminal-specific labeling of osteoclast differentiation factor with a biotin- or fluorophore-containing short peptide on the living cell surface. The labeling reaction occurrs efficiently in serum-containing medium, as well as serum-free medium or PBS. The labeled products are detected after incubation for 5 min. In addition, site-specific proteinprotein conjugation is successfully demonstrated on a living cell surface by the Sortase-catalyzed reaction. This strategy provides a powerful tool for cell biology and cell surface engineering
molecular biology
-
method for immobilizing ligand proteins onto Biacore sensor chips using the transpeptidase activity of Staphylococcus aureus sortase A. This method provides a robust and gentle approach for the site-directed, covalent coupling of proteins to biosensor chips. The high specificity of the sortase allows immobilization of proteins from less than pure protein samples allowing short cuts in protein purification protocols
synthesis
-
in vitro applications of sortase A to protein conjugation. Application of recombinant Staphylococcus aureus sortase A to attach a tagged model protein substrate (green fluorescent protein) to polystyrene beads chemically modified with either alkylamine or the in vivo sortase A ligand, Gly-Gly-Gly, on their surfaces. Sortase A can be used to sequence-specifically ligate eGFP to amino-terminated poly(ethylene glycol) and to generate protein oligomers and cyclized monomers using suitably tagged eGFP An alkylamine can substitute for the natural Gly3 substrate, which suggests the possibility of using the enzyme in materials applications. The highly specific and mild sortase A-catalyzed reaction, based on small recognition tags unlikely to interfere with protein expression represents a useful addition to the protein immobilization and modification tool kit
medicine
-
SrtA contributes to pneumococcal nasopharyngeal colonization in the chinchilla model