Molecular Cloning, Sequence Analysis, and Characterization of a Penicillin-Resistant
            <scp>dd</scp>
            -Carboxypeptidase of
            <i>Myxococcus xanthus</i>

Kimura, Yoshinobu; Takashima, Yukie; Tokumasu, Yushi; Sato, Masayuki

doi:10.1128/jb.181.15.4696-4699.1999

Streptomyces AlbusGD‐Ala‐D‐Ala Carboxypeptidase

Charlier¹,

Wery²,

Dideberg³

et al. 2004

Handbook of Metalloproteins

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The zinc D ‐Ala‐ D ‐Ala carboxypeptidase hydrolyzes the C‐terminal peptide bond of peptides of general structure R‐ D ‐Ala‐ D ‐Xaa. The lytic activity of the enzyme and its extracellular location suggest that it might be used by Streptomyces for fighting competitors in its ecological niche since the enzyme does not hydrolyze the Streptomyces peptidoglycan. The sequence of the 213‐residue mature protein is related to the VanX, VanY, and VanXY proteins of vancomycin‐resistant enterococci. The molecule is an ellipsoid consisting of two globular domains in which the N‐terminal and the C‐terminal ends are pulled apart. The small N‐terminal domain, from residue Asp1 to Pro83, has an all‐α‐helices structure and exhibits a typical three‐helix bundle fold, characteristic of the peptidoglycan binding domain. The largest C‐terminal domain belongs to the α + β type secondary structure, and is related to the N‐terminal domain of the murine sonic hedgehog, a signaling protein involved in natal morphogenesis and formation of embryonic patterning centers, and to the VanX D ‐Ala‐ D ‐Ala dipeptidase of Enterococcus faecium , a protein involved in the vancomycin resistance systems in streptococci. The mixed five‐stranded β‐sheet forms the core of the C‐terminal domain and the lining of one side of the catalytic cavity. One zinc ion occupies a roughly central position in the active site and is coordinated by the His154 NE2, the Asp161 OD1, and the His197 ND1. Classical β‐lactam compounds, which readily inactivate active site serine DD ‐peptidases, are very sluggish inactivators of the zinc D ‐Ala‐ D ‐Ala carboxypeptidase. The best competitive inhibitors are thiol derivatives such as 2‐ and 3‐mercaptopropionate ( K i = 50 and 5 nM) that might behave as bidentate ligands of the Zn 2+ ion.

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Streptomyces AlbusGD‐Ala‐D‐Ala Carboxypeptidase

Charlier

¹

,

Wery

²

,

Dideberg

³

et al. 2004

Encyclopedia of Inorganic and Bioinorganic Chemistry

View full text Add to dashboard Cite

The zinc D ‐Ala‐ D ‐Ala carboxypeptidase hydrolyzes the C‐terminal peptide bond of peptides of general structure R‐ D ‐Ala‐ D ‐Xaa. The lytic activity of the enzyme and its extracellular location suggest that it might be used by Streptomyces for fighting competitors in its ecological niche since the enzyme does not hydrolyze the Streptomyces peptidoglycan. The sequence of the 213‐residue mature protein is related to the VanX, VanY, and VanXY proteins of vancomycin‐resistant enterococci. The molecule is an ellipsoid consisting of two globular domains in which the N‐terminal and the C‐terminal ends are pulled apart. The small N‐terminal domain, from residue Asp1 to Pro83, has an all‐α‐helices structure and exhibits a typical three‐helix bundle fold, characteristic of the peptidoglycan binding domain. The largest C‐terminal domain belongs to the α + β type secondary structure, and is related to the N‐terminal domain of the murine sonic hedgehog, a signaling protein involved in natal morphogenesis and formation of embryonic patterning centers, and to the VanX D ‐Ala‐ D ‐Ala dipeptidase of Enterococcus faecium , a protein involved in the vancomycin resistance systems in streptococci. The mixed five‐stranded β‐sheet forms the core of the C‐terminal domain and the lining of one side of the catalytic cavity. One zinc ion occupies a roughly central position in the active site and is coordinated by the His154 NE2, the Asp161 OD1, and the His197 ND1. Classical β‐lactam compounds, which readily inactivate active site serine DD ‐peptidases, are very sluggish inactivators of the zinc D ‐Ala‐ D ‐Ala carboxypeptidase. The best competitive inhibitors are thiol derivatives such as 2‐ and 3‐mercaptopropionate ( K i = 50 and 5 nM) that might behave as bidentate ligands of the Zn 2+ ion.

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Wide variation in the cyanobacterial complement of presumptive penicillin-binding proteins

Leganés

¹

,

Blanco-Rivero

²

,

Fernández-Piñas

³

et al. 2005

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A genomic analysis of putative penicillin-binding proteins (PBPs) that are involved in the synthesis of the peptidoglycan layer of the cell wall and are encoded in 12 cyanobacterial genomes was performed in order to help elucidate the role(s) of these proteins in peptidoglycan synthesis, especially during cyanobacterial cellular differentiation. The analysis suggested that the minimum set of PBPs needed to assemble the peptidoglycan layer in cyanobacteria probably does not exceed one bifunctional transpeptidase-transglycosylase Class A high-molecular-weight PBP; two Class B high-molecular-weight PBPs, one of them probably involved in cellular elongation and the other in septum formation; and one low-molecular-weight PBP. The low-molecular-weight PBPs of all of the cyanobacteria analyzed are putative endopeptidases and are encoded by fewer genes than in Escherichia coli. We show that in Anabaena sp. strain PCC 7120, predicted proteins All2981 and Alr4579, like Alr5101, are Class A high-molecular-weight PBPs that are required for the functional differentiation of aerobically diazotrophic heterocysts, indicating that some members of this class of PBPs are required specifically for cellular developmental processes.

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Molecular Cloning, Sequence Analysis, and Characterization of a Penicillin-Resistant dd -Carboxypeptidase of Myxococcus xanthus

Cited by 9 publications

References 45 publications

Streptomyces AlbusGD‐Ala‐D‐Ala Carboxypeptidase

Streptomyces AlbusGD‐Ala‐D‐Ala Carboxypeptidase

Streptomyces AlbusGD‐Ala‐D‐Ala Carboxypeptidase

Wide variation in the cyanobacterial complement of presumptive penicillin-binding proteins

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