Ontology highlight
ABSTRACT:
SUBMITTER: Uehara T
PROVIDER: S-EPMC145344 | biostudies-literature | 2003 Jan
REPOSITORIES: biostudies-literature
Uehara Tsuyoshi T Park James T JT
Journal of bacteriology 20030101 2
MpaA amidase was identified in Escherichia coli by its amino acid sequence homology with the ENP1 endopeptidase from Bacillus sphaericus. The enzymatic activity of MpaA, i.e., hydrolysis of the gamma-D-glutamyl-diaminopimelic acid bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, was demonstrated in the cell extract of a strain expressing mpaA from a multicopy plasmid. An mpaA mpl (murein peptide ligase) double mutant accumulated large amounts of murein tripeptide ...[more]