2.3.2.B1: lipid II:alanine alanyl transferase
This is an abbreviated version!
For detailed information about lipid II:alanine alanyl transferase, go to the full flat file.
Reaction
ECTree
Advanced search results
General Information
General Information on EC 2.3.2.B1 - lipid II:alanine alanyl transferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
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
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
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
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
-
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
-
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
-
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
-