(Q59722403)

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An embarrassment of sortases – a richness of substrates? Response

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title

An embarrassment of sortases – a richness of substrates? Response (English)

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Sarkis K Mazmanian

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Hung Ton-That

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Olaf Schneewind

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publication date

March 2001

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published in

Trends in Microbiology

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volume

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issue

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page(s)

101-102

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cites work

Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall

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7 January 2021

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The number of rRNA genes in Escherichia coli

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An Escherichia coli strain with all chromosomal rRNA operons inactivated: complete exchange of rRNA genes between bacteria

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Identification of the major penicillin-binding proteins of Escherichia coli as D-alanine carboxypeptidase IA.

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Mutants of Escherichia coli which lack a component of penicillin-binding protein 1 are viable

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Penicillin-binding proteins and cell shape in E. coli

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

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7 January 2021

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Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Sortase catalyzed in vitro transpeptidation reaction using LPXTG peptide and NH(2)-Gly(3) substrates.

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Sequence homology between the subunits of two immunologically and functionally distinct types of fimbriae of Actinomyces spp

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Cell wall sorting of lipoproteins in Staphylococcus aureus

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7 January 2021

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Biochemistry of bacterial cell envelopes

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7 January 2021

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The Murein-Lipoprotein Linkage in the Cell Wall of Escherichia coli

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Identifiers

DOI

10.1016/S0966-842X(01)01955-2

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