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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

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

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.70 sortase A

Molecular Weight

Molecular Weight on EC 3.4.22.70 - sortase A

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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16595
-
x * 16595, SrtDELTAN59, electrospray ionization mass spectrometry
17800
-
SDS-PAGE
23000
-
SDS-PAGE, immune-reactive species
23900
-
x * 23900, truncated enzyme, calculated from amino acid sequence
24810
25000
-
x * 25000, truncated enzyme, SDS-PAGE
27000
-
x * 27000, SDS-PAGE
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