scholarly journals α∈-Diaminopimelic acid metabolism and sporulation in Bacillus sphaericus

1957 ◽  
Vol 65 (4) ◽  
pp. 700-708 ◽  
Author(s):  
Joan F. Powell ◽  
R. E. Strange
Keyword(s):  
Acid Metabolism ◽  
Bacillus Sphaericus ◽  
Diaminopimelic Acid

scholarly journals Characterization of the sporulation-related γ-d-glutamyl-(l)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 as a member of the metallo(zinc) carboxypeptidase A family. Modular design of the protein

1993 ◽  
Vol 292 (2) ◽  
pp. 563-570 ◽  
Author(s):  
M L Hourdou ◽  
M Guinand ◽  
M J Vacheron ◽  
G Michel ◽  
L Denoroy ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Modular Design ◽  
Catalytic Domain ◽  
Specific Activity ◽  
Protein A ◽  
Bacillus Sphaericus ◽  
Diaminopimelic Acid ◽  
Carboxypeptidase A ◽  
Terminal Repeats

The sporulation-related gamma-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 has been analysed by proton-induced X-ray emission. It contains 1 equivalent Zn2+ per mol of protein. As derived from gene cloning and sequencing, the B. sphaericus Zn peptidase I is a two-module protein. A 100-amino-acid-residue N-terminal domain consisting of two tandem segments of similar sequences, is fused to a 296-amino-acid-residue C-terminal catalytic domain. The catalytic domain belongs to the Zn carboxypeptidase A family, the closest match being observed with the Streptomyces griseus carboxypeptidase [Narahashi (1990) J. Biochem. 107, 879-886] and with the family prototype, bovine carboxypeptidase A. The catalytic domain of the B. sphaericus peptidase I possesses, distributed along the amino-acid sequence, peptide segments, a triad His162-Glu165-His307 and a dyad Tyr347-Glu366 that are equivalent to secondary structures, the zinc-binding triad His69-Glu72-His196 and the catalytic dyad Tyr248-Glu270 of bovine carboxypeptidase A respectively. The N-terminal repeats of the B. sphaericus peptidase I have similarity with the C-terminal repeats of the Enterococcus hirae muramidase 2, the Streptococcus (now Enterococcus) faecalis autolysin and the Bacillus phi PZA and phi 29 lysozymes, to which a role in the recognition of a particular moiety of the bacterial cell envelope has been tentatively assigned. Detergents enhance considerably the specific activity of the B. sphaericus peptidase I.

scholarly journals Identification of MpaA, an Amidase in Escherichia coli That Hydrolyzes the γ-d-Glutamyl-meso-Diaminopimelate Bond in Murein Peptides

2003 ◽  
Vol 185 (2) ◽  
pp. 679-682 ◽  
Author(s):  
Tsuyoshi Uehara ◽  
James T. Park
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Double Mutant ◽  
Biosynthetic Pathway ◽  
Bacillus Sphaericus ◽  
Cell Extract ◽  
Diaminopimelic Acid ◽  
Multicopy Plasmid ◽  
Amino Acid Sequence Homology ◽  
Hydrolysis Of

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 γ-d-glutamyl-diaminopimelic acid bond in the murein tripeptide l-alanyl-γ-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.

Amino Acid Metabolism

1979 ◽  
Vol 7 (1) ◽  
pp. 261-262
Author(s):  
E. V. ROWSELL
Keyword(s):  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism

Effect of intravenous bicarbonate administration on postoperative amino acid metabolism

1985 ◽  
Vol 4 ◽  
pp. 141-146 ◽  
Author(s):  
K VESTERBERG ◽  
J BERGSTROM ◽  
P FURST ◽  
U LEANDER ◽  
E VINNARS
Keyword(s):  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism
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