Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow.
about
Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triadStructure of the LdcB LD-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan RecognitionStructural elucidation of the Cys-His-Glu-Asn proteolytic relay in the secreted CHAP domain enzyme from the human pathogenStaphylococcus saprophyticusStructure and function of a serine carboxypeptidase adapted for degradation of the protein synthesis antibiotic microcin C7Structural and Functional Characterization of Microcin C Resistance Peptidase MccF from Bacillus anthracisStructure and Function of a Novel LD-Carboxypeptidase A Involved in Peptidoglycan RecyclingUnconventional serine proteases: variations on the catalytic Ser/His/Asp triad configurationAphids acquired symbiotic genes via lateral gene transferThe natural history of molecular functions inferred from an extensive phylogenomic analysis of gene ontology dataThe Cell Shape-determining Csd6 Protein from Helicobacter pylori Constitutes a New Family of L,D-Carboxypeptidase.Specificity of L,D-transpeptidases from gram-positive bacteria producing different peptidoglycan chemotypes.Peptidoglycan structure analysis of Lactococcus lactis reveals the presence of an L,D-carboxypeptidase involved in peptidoglycan maturation.Intestine may be a major site of action for the apoA-I mimetic peptide 4F whether administered subcutaneously or orally.Characterization of mutants deficient in the L,D-carboxypeptidase (DacB) and WalRK (VicRK) regulon, involved in peptidoglycan maturation of Streptococcus pneumoniae serotype 2 strain D39.Identification and characterization of a novel serine protease, VvpS, that contains two functional domains and is essential for autolysis of Vibrio vulnificusCharacterization of structural variations in the peptidoglycan of vancomycin-susceptible Enterococcus faecium: understanding glycopeptide-antibiotic binding sites using mass spectrometry.Bacterial peptidoglycan (murein) hydrolases.How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)Peptidoglycan LD-carboxypeptidase Pgp2 influences Campylobacter jejuni helical cell shape and pathogenic properties and provides the substrate for the DL-carboxypeptidase Pgp1.A Single Dual-Function Enzyme Controls the Production of Inflammatory NOD Agonist Peptidoglycan Fragments by Neisseria gonorrhoeae.
P2860
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P2860
Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow.
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Pseudomonas aeruginosa LD-carb ...... riad and a nucleophilic elbow.
@ast
Pseudomonas aeruginosa LD-carb ...... riad and a nucleophilic elbow.
@en
type
label
Pseudomonas aeruginosa LD-carb ...... riad and a nucleophilic elbow.
@ast
Pseudomonas aeruginosa LD-carb ...... riad and a nucleophilic elbow.
@en
prefLabel
Pseudomonas aeruginosa LD-carb ...... riad and a nucleophilic elbow.
@ast
Pseudomonas aeruginosa LD-carb ...... riad and a nucleophilic elbow.
@en
P2860
P356
P1476
Pseudomonas aeruginosa LD-carb ...... riad and a nucleophilic elbow.
@en
P2093
Henryk J Korza
P2860
P304
40802-40812
P356
10.1074/JBC.M506328200
P407
P577
2005-09-14T00:00:00Z