Open AccessCharacterization of three different lytic transglycosylases in Escherichia coli
Author(s) -
Romeis Tina,
Vollmer Waldemar,
Höltje JoachimVolker
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06376.x
Subject(s) - lytic cycle , escherichia coli , biochemistry , enzyme , mutant , glycan , chemistry , biology , gene , glycoprotein , virus , virology
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.