ExplorEnz: EC 3.4.22.70

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3.4.22.70

Accepted name:

sortase A

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.

Other name(s):

SrtA; SrtA protein; SrtA sortase

Comments:

In peptidase family C60.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB

References:

1.	Ton-That, H., Liu, G., Mazmanian, S.K., Faull, K.F. and Schneewind, O. Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif. Proc. Natl. Acad. Sci. USA 96 (1999) 12424–12429. [DOI] [PMID: 10535938]
2.	Zong, Y., Bice, T.W., Ton-That, H., Schneewind, O. and Narayana, S.V. Crystal structures of Staphylococcus aureus sortase A and its substrate complex. J. Biol. Chem. 279 (2004) 31383–31389. [DOI] [PMID: 15117963]
3.	Race, P.R., Bentley, M.L., Melvin, J.A., Crow, A., Hughes, R.K., Smith, W.D., Sessions, R.B., Kehoe, M.A., McCafferty, D.G. and Banfield, M.J. Crystal structure of Streptococcus pyogenes sortase A: implications for sortase mechanism. J. Biol. Chem. 284 (2009) 6924–6933. [DOI] [PMID: 19129180]

[EC 3.4.22.70 created 2009]