KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.02 | - |
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-2,4-dinitrophenyl ester | hydrolysis reaction | Staphylococcus aureus | |
0.041 | - |
Gly-Gly-Gly | pH 7.5, transpeptidation with o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-2,4-dinitrophenol | Staphylococcus aureus | |
0.117 | - |
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-2,4-dinitrophenyl ester | pH 7.5, transpeptidation with Gly-Gly-Gly | Staphylococcus aureus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Staphylococcus aureus | 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 | ? | - |
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Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | Staphylococcus aureus | ? | - |
? | |
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 | Staphylococcus aureus | ? | - |
? | |
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-2,4-dinitrophenyl ester + Gly-Gly-Gly | 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 | Staphylococcus aureus | o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-Gly-Gly + Gly-2,4-dinitrophenyl ester | - |
? | |
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-2,4-dinitrophenyl ester + H2O | 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 | Staphylococcus aureus | o-aminobenzoyl-Leu-Pro-Glu-Thr + Gly-2,4-dinitrophenyl ester | - |
? |