A substitution at His-120 in the LasA protease of Pseudomonas aeruginosa blocks enzymatic activity without affecting propeptide processing or extracellular secretion
about
Molecular and biotechnological aspects of microbial proteasesCrystal Structure of Outer Membrane Protein NMB0315 from Neisseria meningitidisIdentification of a chitin-binding protein secreted by Pseudomonas aeruginosaPseudomonas aeruginosa possesses two putative type I signal peptidases, LepB and PA1303, each with distinct roles in physiology and virulenceSecretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa.Mutation of the zinc-binding metalloprotease motif affects Bacteroides fragilis toxin activity but does not affect propeptide processing.Bacteriophage Tuc2009 encodes a tail-associated cell wall-degrading activity.Full activation of Enterococcus faecalis gelatinase by a C-terminal proteolytic cleavage.A sporulation membrane protein tethers the pro-sigmaK processing enzyme to its inhibitor and dictates its subcellular localizationPurification and molecular characterization of glycylglycine endopeptidase produced by Staphylococcus capitis EPK1.Identification of critical residues in the propeptide of LasA protease of Pseudomonas aeruginosa involved in the formation of a stable mature protease.A feeding tube model for activation of a cell-specific transcription factor during sporulation in Bacillus subtilis.Pseudomonas aeruginosa LasA protease in treatment of experimental staphylococcal keratitis.Extracellular metalloproteases from bacteria.Peptidoglycan hydrolases-potential weapons against Staphylococcus aureusRedox-Sensitive MarR Homologue BifR from Burkholderia thailandensis Regulates Biofilm Formation.Activity of the type I signal peptidase inhibitor MD3 against multidrug-resistant Gram-negative bacteria alone and in combination with colistin.Enterolysin A, a cell wall-degrading bacteriocin from Enterococcus faecalis LMG 2333.Similar active sites in lysostaphins and D-Ala-D-Ala metallopeptidases.
P2860
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P2860
A substitution at His-120 in the LasA protease of Pseudomonas aeruginosa blocks enzymatic activity without affecting propeptide processing or extracellular secretion
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
A substitution at His-120 in t ...... ing or extracellular secretion
@ast
A substitution at His-120 in t ...... ing or extracellular secretion
@en
type
label
A substitution at His-120 in t ...... ing or extracellular secretion
@ast
A substitution at His-120 in t ...... ing or extracellular secretion
@en
prefLabel
A substitution at His-120 in t ...... ing or extracellular secretion
@ast
A substitution at His-120 in t ...... ing or extracellular secretion
@en
P2093
P2860
P1476
A substitution at His-120 in t ...... ing or extracellular secretion
@en
P2093
P2860
P304
P356
10.1128/JB.178.22.6608-6617.1996
P407
P577
1996-11-01T00:00:00Z