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Characterization of three different lytic transglycosylases in Escherichia coli

Lookup NU author(s): Professor Waldemar Vollmer


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Abstract Two lytic transglycosylases, releasing 1,6-anhydromuropeptides from murein sacculi are present in a mutant deleted for the soluble lytic transglycosylase 70 (Slt70). Thus, there are three different lytic transglycosylases in Escherichia coli. One of the remaining enzymes is soluble and one is a membrane protein that can be solubilized by 2% Triton X-100 in 0.5 M NaCl. Both enzymes are exo-muramidases. Only the membrane enzyme, but not the soluble ones, hydrolyses isolated murein glycan strands (poly-GlcNAc-MurNAc). While the soluble enzymes are inhibited by the muropeptide TetraTriLysArg(dianhydro), the membrane enzyme is not. The antibiotic bulgecin that inhibits Slt70 does not inhibit the lytic transglycosylases present in the slt70 deletion mutant.

Publication metadata

Author(s): Romeis T, Vollmer W, Höltje J-V

Publication type: Article

Publication status: Published

Journal: FEMS Microbiology Letters

Year: 1993

Volume: 111

Issue: 2-3

Pages: 141-146

ISSN (print): 0378-1097

ISSN (electronic): 1574-6968

Publisher: Wiley-Blackwell Publishing Ltd.


DOI: 10.1111/j.1574-6968.1993.tb06376.x


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