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Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif

Ton-That, Hung and Liu, Gwen and Mazmanian, Sarkis K. and Faull, Kym F. and Schneewind, Olaf (1999) Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif. Proceedings of the National Academy of Sciences of the United States of America, 96 (22). pp. 12424-12429. ISSN 0027-8424. PMCID PMC22937. doi:10.1073/pnas.96.22.12424.

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Surface proteins of Staphylococcus aureus are linked to the bacterial cell wall by sortase, an enzyme that cleaves polypeptides at the threonine of the LPXTG motif. Surface proteins can be released from staphylococci by treatment with hydroxylamine, resulting in the formation of threonine hydroxamate. Staphylococcal extracts, as well as purified sortase, catalyze the hydroxylaminolysis of peptides bearing an LPXTG motif, a reaction that can be inhibited with sulfhydryl-modifying reagents. Replacement of the single conserved cysteine at position 184 of sortase with alanine abolishes enzyme activity. Thus, sortase appears to catalyze surface-protein anchoring by means of a transpeptidation reaction that captures cleaved polypeptides as thioester enzyme intermediates.

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Mazmanian, Sarkis K.0000-0003-2713-1513
Additional Information:© 1999 by The National Academy of Sciences Edited by Christopher T. Walsh, Harvard Medical School, Boston, MA, and approved September 1, 1999 (received for review June 23, 1999) We thank Drs. Dominique Missiakas [University of California, Los Angeles (UCLA)], Peter Model, Marjorie Russel (Rockefeller University), and members of our laboratory for discussion and critical reading of this manuscript. H.T.T. was supported by the Predoctoral Training Program in Microbial Pathogenesis at UCLA (AI07323). S.K.M. was supported by the Predoctoral Training Program in Genetic Mechanisms at UCLA (T32GM07104). The W. M. Keck Foundation provided support toward instrument purchase. Work in the laboratory of O.S. is supported by Grant AI33987 from the National Institutes of Health-National Institute of Allergy and Infectious Diseases, Infectious Disease Branch. This paper was submitted directly (Track II) to the PNAS office. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Funding AgencyGrant Number
NIH Predoctoral FellowshipAI07323
NIH Predoctoral FellowshipT32GM07104
W. M. Keck FoundationUNSPECIFIED
National Institute of Allergy and Infectious DiseasesUNSPECIFIED
Issue or Number:22
PubMed Central ID:PMC22937
Record Number:CaltechAUTHORS:TONpnas99
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:6021
Deposited By: Archive Administrator
Deposited On:14 Nov 2006
Last Modified:08 Nov 2021 20:30

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