Journal
JOURNAL OF BACTERIOLOGY
Volume 185, Issue 2, Pages 679-682Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.185.2.679-682.2003
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Funding
- NIGMS NIH HHS [GM51610, R01 GM051610] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM051610] Funding Source: NIH RePORTER
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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 in its cytoplasm, consistent with the premise that MpaA degrades the tripeptide if its recycling via the peptidoglycan biosynthetic pathway is blocked.
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