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Literature summary extracted from

  • Filipe, s.R.; Pinho, M.G.; Tomasz, A.
    Characterization of the murMN operon involved in the synthesis of branched peptidoglycan peptides in Streptococcus pneumoniae (2000), J. Biol. Chem., 275, 27768-27774.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.B1 Streptococcus pneumoniae Q9K307 penicillin-resistant strain
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2.3.2.B1 Streptococcus pneumoniae Q9L447 penicillin-susceptible strain
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2.3.2.B1 Streptococcus pneumoniae Pen6 Q9K307 penicillin-resistant strain
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2.3.2.B1 Streptococcus pneumoniae R36A Q9L447 penicillin-susceptible strain
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2.3.2.B2 Streptococcus pneumoniae Q9L445 penicillin-resistant strain
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2.3.2.B2 Streptococcus pneumoniae Pen6 Q9L445 penicillin-resistant strain
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General Information

EC Number General Information Comment Organism
2.3.2.B1 physiological function allelic replacement of the mosaic murM gene of strain Pen6 with murM of the penicillin-susceptible laboratory strain R36A causes enrichment of the peptidoglycan in linear muropeptides Streptococcus pneumoniae
2.3.2.B1 physiological function inactivation of the murMN operon by insertion duplication mutagenesis does not cause any significant change in growth rate of the cultures, but leads to the disappearance of all branched muropeptide monomers and dimers accompanied by a parallel increase in the percentage of linear structured stem peptides and in the appearance of novel peptide structures. Allelic replacement of the mosaic murM gene of strain Pen6 with murM of the penicillin-susceptible laboratory strain R36A causes enrichment of the peptidoglycan in linear muropeptides Streptococcus pneumoniae
2.3.2.B2 physiological function selective inactivation of the murN gene causes production of an unusual peptidoglycan that contains only single amino acid residues in the muropeptide branches Streptococcus pneumoniae