Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
about
Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimmingDiscovery of α,β- and α,γ-diamino acid scaffolds for the inhibition of M1 family aminopeptidasesA Naturally Variable Residue in the S1 Subsite of M1 Family Aminopeptidases Modulates Catalytic Properties and Promotes Functional SpecializationTma108, a putative M1 aminopeptidase, is a specific nascent chain-associated protein in Saccharomyces cerevisiae.Characterization of a Vibrio fischeri aminopeptidase and evidence for its influence on an early stage of squid colonizationEnzymatic synthesis of bioinformatically predicted microcin C-like compounds encoded by diverse bacteria.Purification and functional characterisation of rhiminopeptidase A, a novel aminopeptidase from the venom of Bitis gabonica rhinoceros.Aminopeptidase N1 (EtAPN1), an M1 metalloprotease of the apicomplexan parasite Eimeria tenella, participates in parasite development.An integrated approach to the ligand binding specificity of Neisseria meningitidis M1 alanine aminopeptidase by fluorogenic substrate profiling, inhibitory studies and molecular modeling.The role of multifunctional M1 metallopeptidases in cell cycle progressionStructure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.Structural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N.Engagement of the S1, S1' and S2' subsites drives efficient catalysis of peptide bond hydrolysis by the M1-family aminopeptidase from Plasmodium falciparum.Intestinal peptidases form functional complexes with the neutral amino acid transporter B(0)AT1.Aminoacyl β-naphthylamides as substrates and modulators of AcrB multidrug efflux pumpInsight into the remarkable affinity and selectivity of the aminobenzosuberone scaffold for the M1 aminopeptidases family based on structure analysis.Glu121-Lys319 salt bridge between catalytic and N-terminal domains is pivotal for the activity and stability of Escherichia coli aminopeptidase N.Two cap residues in the S1 subsite of a Plasmodium falciparum M1-family aminopeptidase promote broad specificity and enhance catalysis.Combinatorial multicomponent access to natural-products-inspired peptidomimetics: discovery of selective inhibitors of microbial metallo-aminopeptidases.
P2860
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P2860
Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
description
2008 nî lūn-bûn
@nan
2008 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2008年の論文
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2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
@ast
Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
@en
Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
@nl
type
label
Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
@ast
Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
@en
Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
@nl
prefLabel
Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
@ast
Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
@en
Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
@nl
P2093
P3181
P356
P1433
P1476
Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
@en
P2093
Anthony Addlagatta
Brian W Matthews
Leslie Gay
P304
P3181
P356
10.1021/BI7022333
P407
P577
2008-05-13T00:00:00Z