EC Number   |
General Information |
Reference |
|---|
    3.4.16.4 | malfunction |
loss of penicillin-binding protein 5 enhances beta-lactam susceptibility, the observed susceptibilities for ampicillin, piperacillin, amoxicillin, penicillin G, cefadroxil and cefalexin are enhanced by 4fold and for cefalothin and cefaclor the susceptibilities are at least 8fold higher in the mutants |
708741 |
| 3.4.16.4 | physiological function |
D,D-CPases PBP5, PBP6a, and PBP6b change dimer conformation between resting and active states. The isoforms are not redundant but that their balanced activity is required for robust peptidoglycan synthesis |
754599 |
| 3.4.16.4 | physiological function |
enzyme has a role in removing the last D-Ala from the pentapeptide peptidoglycan precursors and reprogramming cell wall biosynthesis. Isoform C-His6-VanYn over-expression confers glycopeptide resistance to Streptomyces venezuelae. The addition of His6-tag at the N-terminus of the protein abolishes its biological activity either in vitro or in vivo assays |
-, 731544 |
| 3.4.16.4 | physiological function |
in a gene disruption mutant, the spores are affected in their resistance to heat and acid and show a dramatic increase in swelling during germination. The mycelium of the mutant is more sensitive to glycopeptide antibiotics vancomycin and teicoplanin. Both the DD-CPase domain and the hydrophobic transmembrane region are essential for complementing the wild type phenotypes in the mutant. In a model for the biological mechanism, DD-CPase releases D-Ala from peptidoglycan precursors, thereby reducing the substrate pool for peptidoglycan crosslinking (transpeptidation) |
-, 755422 |
| 3.4.16.4 | physiological function |
in an isoform DacC deletion mutant, the extracellular activities and fluorescence value of recombinant amylase, green fluorescent protein, and alpha-galactosidase are increased by 82.3, 29.1, and 37.7%, respectively, compared with that of control cells. The outer membrane permeability and intracellular soluble peptidoglycan accumulation of the deletion mutant are also enhanced. In the poles of the deletion mutant, local transparent bulges are found |
753439 |
| 3.4.16.4 | physiological function |
overexpression of D,D-carboxypeptidase DacA or DacB promotes the accumulation of intracellular soluble peptidoglycan, alters cell morphology (shape and size) and leads to the formation of transparent globular structures in Escherichia coli cells. Extracellular production of recombinant green fluorescent protein is increased by 1.7- and 2.3fold upon overexpression of DacA and DacB, respectively. Extracellular production of recombinant amylase and apha-galactosidase is increased by 4.5- and 2.8fold, respectively, upon overexpression of DacA, and by 11.9- and 2.5fold, respectively, upon overexpression of DacB. Overexpression of DacA or DacB enhances both the outer and inner membrane permeability of Escherichia coli |
752575 |
| 3.4.16.4 | physiological function |
peptide uptake transporters BclA and DD-CPase1 act independently in the morphological differentiation of bacteroids induced by Nodule-specific Cysteine-Rich peptides NCR. The nitrogenase activity of plants infected with a DD-CPase1 mutant is strongly reduced, in large part because the mutant induces much less nodules than the wild type. A BclA/DD-CPAse1 double exhibits a similar symbiotic phenotype as the DD-CPase1 single mutant |
-, 755483 |
| 3.4.16.4 | physiological function |
the beta-lactam-sensitive D,D-carboxypeptidase activity of Pbp4 controls the L,D and D,D transpeptidation pathways in Corynebacterium jeikeium |
709996 |
| 3.4.16.4 | physiological function |
the DD-carboxypeptidase activity of PBP 5 is responsible for maintaining cell shape |
708523 |
| 3.4.16.4 | physiological function |
Vibrio cholerae lacking isoform DacA-1 displays slow growth, aberrant morphology and altered peptidoglycan homeostasis in Luria-Bertani medium, as well as a profound plating defect. DacA-1 alone among Vibrio choleraes low molecular weight penicillin-binding proteins is critical for bacterial growth. The growth and morphology of the dacA-1 mutant are unimpaired in Luria-Bertani media containing reduced concentrations of NaCl of 100 mM or less, and also within suckling mice, a model host for the study of cholera pathogenesis. Peptidoglycan from the dacA-1 mutant contains elevated pentapeptidelevels in standard and low salt media |
-, 731725 |
