Open Access
,
volume 96
,
issue 22
,
pages 12424-12429
Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif
Publication type: Journal Article
Publication date: 1999-10-26
scimago Q1
wos Q1
SJR: 3.414
CiteScore: 16.5
Impact factor: 9.1
ISSN: 00278424, 10916490
PubMed ID:
10535938
Multidisciplinary
Abstract
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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514
Total citations:
514
Citations from 2025:
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(3.31%)
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Cite this
GOST
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Ton-That H. et al. 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. 1999. Vol. 96. No. 22. pp. 12424-12429.
GOST all authors (up to 50)
Copy
Ton-That H., Liu G., Mazmanian S. K., FAULL K. F., Schneewind O. 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. 1999. Vol. 96. No. 22. pp. 12424-12429.
Cite this
RIS
Copy
TY - JOUR
DO - 10.1073/pnas.96.22.12424
UR - https://doi.org/10.1073/pnas.96.22.12424
TI - Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif
T2 - Proceedings of the National Academy of Sciences of the United States of America
AU - Ton-That, Hung
AU - Liu, Gwen
AU - Mazmanian, Sarkis K.
AU - FAULL, KYM F.
AU - Schneewind, Olaf
PY - 1999
DA - 1999/10/26
PB - Proceedings of the National Academy of Sciences (PNAS)
SP - 12424-12429
IS - 22
VL - 96
PMID - 10535938
SN - 0027-8424
SN - 1091-6490
ER -
Cite this
BibTex (up to 50 authors)
Copy
@article{1999_Ton-That,
author = {Hung Ton-That and Gwen Liu and Sarkis K. Mazmanian and KYM F. FAULL and Olaf Schneewind},
title = {Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
year = {1999},
volume = {96},
publisher = {Proceedings of the National Academy of Sciences (PNAS)},
month = {oct},
url = {https://doi.org/10.1073/pnas.96.22.12424},
number = {22},
pages = {12424--12429},
doi = {10.1073/pnas.96.22.12424}
}
Cite this
MLA
Copy
Ton-That, Hung, et al. “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, vol. 96, no. 22, Oct. 1999, pp. 12424-12429. https://doi.org/10.1073/pnas.96.22.12424.