Premium
A novel glycan polymerase that synthesizes uncross‐linked peptidoglycan in Escherichia coli
Author(s) -
Hara Hiroshi,
Suzuki Hideho
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80226-4
Subject(s) - glycan , peptidoglycan , escherichia coli , biochemistry , polymerase , penicillin binding proteins , chemistry , biology , enzyme , gene , glycoprotein
A simple and efficient procedure to assay peptidoglycan synthesis in vitro was established. By this procedure, a novel activity for glycan polymerization in Escherichia coli was found in the fraction containing no detectable penicillin‐binding protein (PBP). This polymerase activity was relatively insensitive to moenomycin, showed requirement for Ca 2+ or Mn 2+ but not for Mg 2+ , and led to production of uncross‐linked glycan chains. These properties distinguished the glycan polymerase from the activities shown by the fractions containing PBPs. The glycan polymerase catalyzing polymerization of glycan units from lipid intermediates was purified and identified as a protein of 34 kDa.