Identification of MpaA, an amidase in Escherichia coli that hydrolyzes the gamma-D-glutamyl-meso-diaminopimelate bond in murein peptides - PubMed (original) (raw)

Identification of MpaA, an amidase in Escherichia coli that hydrolyzes the gamma-D-glutamyl-meso-diaminopimelate bond in murein peptides

Tsuyoshi Uehara et al. J Bacteriol. 2003 Jan.

Abstract

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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Figures

FIG. 1.

Alignment of the amino acid sequences of the ENP1 endopeptidase from B. sphaericus and YcjI (MpaA) from E. coli by T-COFFEE program (

http://www.ch.embnet.org/software/TCoffee.html

). Identical amino acids and conserved amino acids are indicated by stars and colons, respectively. Amino acid numbers for both proteins are indicated on the right. ENP1 and YcjI sequences are referred to as Q03415 and P51983 in the Swiss-Prot library. The putative zinc binding triad His162-Glu165-His307, catalytic dyad Tyr347-Glu366, and substrate binding residue Asp255 of ENP1 are underlined.

FIG. 2.

HPLC analysis of hot-water extracts of E. coli wild type, the mpl::Kan mutant, the mpaA::Cm mutant, and the double mutant. As described in the text, cells were labeled with [3H]Dap at 37°C and harvested at mid-log phase. All values are corrected by the cell turbidity (5 ml of culture, 100 Klett units). Fraction A, Dap; fraction B,

-Ala-γ-

-Glu-Dap; fraction C, UDP-MurNAc-pentapeptide.

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Identification of MpaA, an amidase in Escherichia coli that hydrolyzes the gamma-D-glutamyl-meso-diaminopimelate bond in murein peptides - PubMed (original) (raw)