3.4.22.70: sortase A
This is an abbreviated version!
For detailed information about sortase A, go to the full flat file.
Word Map on EC 3.4.22.70
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3.4.22.70
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aureus
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staphylococcus
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lpxtg
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streptococcus
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peptidoglycan
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transpeptidation
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sortase-mediated
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a-mediated
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adhesins
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bioconjugation
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antivirulence
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mutans
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anti-infective
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pilins
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transpeptidases
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oligoglycine
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cross-bridges
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pentaglycine
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wall-anchored
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molecular biology
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azide-alkyne
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analysis
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biotechnology
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drug development
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synthesis
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medicine
- 3.4.22.70
- aureus
- staphylococcus
-
lpxtg
- streptococcus
- peptidoglycan
-
transpeptidation
-
sortase-mediated
-
a-mediated
- adhesins
-
bioconjugation
-
antivirulence
- mutans
-
anti-infective
- pilins
- transpeptidases
-
oligoglycine
-
cross-bridges
- pentaglycine
-
wall-anchored
- molecular biology
-
azide-alkyne
- analysis
- biotechnology
- drug development
- synthesis
- medicine
Reaction
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. =
Synonyms
C60.001, sortase A, sortase A transpeptidase, sortase SrtA, sortase transpeptidase, SrtA, SrtA protein, SrtA sortase
ECTree
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Application
Application on EC 3.4.22.70 - sortase A
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analysis
biotechnology
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the bacterial transpeptidase sortase A is a well-established tool in protein chemistry and catalyzes the chemoselective ligation of peptides and proteins
drug development
medicine
molecular biology
synthesis
additional information
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development of a reverse-phase HPLC assay to identify and characterize sortase reaction intermediates
analysis
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semisynthetic active site mutant enzymes containing selenocysteine and homocysteine might represent useful tools for further biochemical investigations and engineering approaches of sortases A
drug development
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the enzyme is is a promising target for therapies against Gram-positive bacteria, in general, and staphylococci, in particular
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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
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
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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
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SrtA activity is a prime target for inhibition of Staphylococcus aureus colonization
medicine
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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
medicine
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SrtA contributes to pneumococcal nasopharyngeal colonization in the chinchilla model
medicine
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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
medicine
the mutant strain TBY-1DELTAsrtA is used as a live vaccine, which is administered via intraperitoneal injection. It provides the relative percent survival value of 95.5% in Nile tilapia, thereby demonstrating its high potential as an effective attenuated live vaccine candidate
medicine
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the mutant strain TBY-1DELTAsrtA is used as a live vaccine, which is administered via intraperitoneal injection. It provides the relative percent survival value of 95.5% in Nile tilapia, thereby demonstrating its high potential as an effective attenuated live vaccine candidate
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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
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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
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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
synthesis
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semienzymatic cyclization of disulfide-rich peptides using sortase A, overview
synthesis
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the bacterial transpeptidase sortase A is a well-established tool in protein chemistry and catalyzes the chemoselective ligation of peptides and proteins
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sortase A mediates site-specific immobilization for identification of protein interactions in affinity purification-mass spectrometry experiments, overview. the enzyme is used for proteins or peptide baits with a C-terminal LPXTG recognition motif that are covalently immobilized to beads carrying an oligoglycine peptide (nucleophile). Tryptic on-bead digestion and spike-in of a heavy isotope labeled reference peptide (13C515N1-Val) allows for the absolute quantification of immobilized peptide or protein by MALDI-MS, method overview
additional information
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Staphylococcus aureus sortase A is a transpeptidase that is extensively used in various protein research applications, the enzyme is highly selective and does not require any cofactors for the catalysis of protein ligation and can be produced in high yields
additional information
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Staphylococcus aureus sortase A is a transpeptidase that is extensively used in various protein research applications, the enzyme is highly selective and does not require any cofactors for the catalysis of protein ligation and can be produced in high yields
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