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Literature summary for 3.4.22.70 extracted from

  • Huang, X.; Aulabaugh, A.; Ding, W.; Kapoor, B.; Alksne, L.; Tabei, K.; Ellestad, G.
    Kinetic mechanism of Staphylococcus aureus sortase SrtA (2003), Biochemistry, 42, 11307-11315.
    View publication on PubMed
Search for more literature for 3.4.22.70

KM Value [mM]

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/ Products (Substrates)

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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-

Substrates and Products (Substrate)

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
-
 ?