dacD, an Escherichia coli gene encoding a novel penicillin-binding protein (PBP6b) with DD-carboxypeptidase activity.
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Contribution of membrane-binding and enzymatic domains of penicillin binding protein 5 to maintenance of uniform cellular morphology of Escherichia coli.Bacillus subtilis cells lacking penicillin-binding protein 1 require increased levels of divalent cations for growth.Beta-lactam antibiotics: from antibiosis to resistance and bacteriologypbpB, a gene coding for a putative penicillin-binding protein, is required for aerobic nitrogen fixation in the cyanobacterium Anabaena sp. strain PCC7120.Contributions of PBP 5 and DD-carboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli.Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent.A weak DD-carboxypeptidase activity explains the inability of PBP 6 to substitute for PBP 5 in maintaining normal cell shape in Escherichia coli.Bacterial cell wall synthesis: new insights from localization studiesSequences near the active site in chimeric penicillin binding proteins 5 and 6 affect uniform morphology of Escherichia coli.Peptidoglycan hydrolases of Escherichia coli.Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis.AmpC and AmpH, proteins related to the class C beta-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli.The Redundancy of Peptidoglycan Carboxypeptidases Ensures Robust Cell Shape Maintenance in Escherichia coliRole of penicillin-binding proteins in the initiation of the AmpC beta-lactamase expression in Enterobacter cloacae.Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis.Penicillin binding protein 5 affects cell diameter, contour, and morphology of Escherichia coli.Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli.AmpH, a bifunctional DD-endopeptidase and DD-carboxypeptidase of Escherichia coli.Impacts of Penicillin Binding Protein 2 Inactivation on β-Lactamase Expression and Muropeptide Profile in Stenotrophomonas maltophilia.Low-molecular-mass penicillin binding protein 6b (DacD) is required for efficient GOB-18 metallo-β-lactamase biogenesis in Salmonella enterica and Escherichia coli.Response of extraintestinal pathogenic Escherichia coli to human serum reveals a protective role for Rcs-regulated exopolysaccharide colanic acid.Neisseria gonorrhoeae penicillin-binding protein 3 demonstrates a pronounced preference for N(epsilon)-acylated substrates.High binding affinity of repressor IolR avoids costs of untimely induction of myo-inositol utilization by Salmonella Typhimurium.Overexpression and enzymatic characterization of Neisseria gonorrhoeae penicillin-binding protein 4.Moderate deacylation efficiency of DacD explains its ability to partially restore beta-lactam resistance in Escherichia coli PBP5 mutant.Investigations into the mechanisms used by the C-terminal anchors of Escherichia coli penicillin-binding proteins 4, 5, 6 and 6b for membrane interaction.The gene bolA regulates dacA (PBP5), dacC (PBP6) and ampC (AmpC), promoting normal morphology in Escherichia coli.Francisella tularensis D-Ala D-Ala Carboxypeptidase DacD Is Involved in Intracellular Replication and It Is Necessary for Bacterial Cell Wall Integrity.The Fluorescent D-Amino Acid NADA as a Tool to Study the Conditional Activity of Transpeptidases in
P2860
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P2860
dacD, an Escherichia coli gene encoding a novel penicillin-binding protein (PBP6b) with DD-carboxypeptidase activity.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
dacD, an Escherichia coli gene ...... DD-carboxypeptidase activity.
@ast
dacD, an Escherichia coli gene ...... DD-carboxypeptidase activity.
@en
type
label
dacD, an Escherichia coli gene ...... DD-carboxypeptidase activity.
@ast
dacD, an Escherichia coli gene ...... DD-carboxypeptidase activity.
@en
prefLabel
dacD, an Escherichia coli gene ...... DD-carboxypeptidase activity.
@ast
dacD, an Escherichia coli gene ...... DD-carboxypeptidase activity.
@en
P2093
P2860
P1476
dacD, an Escherichia coli gene ...... DD-carboxypeptidase activity.
@en
P2093
P2860
P304
P356
10.1128/JB.178.24.7106-7111.1996
P407
P577
1996-12-01T00:00:00Z