EC Number   |
General Information |
Reference |
|---|
  2.3.2.B1 | physiological function |
adds L-serine or L-alanine as the first amino acid of a dipeptide branch to the stem peptide lysine of the pneumococcal peptidoglycan. MurM activity is essential for clinical pneumococcal penicillin resistance |
-, 712366 |
| 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 |
-, 712344 |
| 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 |
-, 712344 |
| 2.3.2.B1 | physiological function |
the muropeptide composition of the pneumococcal cell walls is determined by the particular murM allele carried by the cells. After cloning of different murM alleles from several penicillin-resistant Streptococcus pneumoniae strains, each with a characteristic branched peptide pattern, and transformation into the penicillin-susceptible laboratory strain R36A, all transformants remain penicillin-susceptible, their cell wall composition changing in directions corresponding to the muropeptide pattern of the strain from which the murM allele is derived |
712350 |
