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Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translationThe anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidaseThe two authentic methionine aminopeptidase genes are differentially expressed in Bacillus subtilis.Inhibition of Monometalated Methionine Aminopeptidase: Inhibitor Discovery and Crystallographic Analysis †Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymesDiscovery of Inhibitors of Escherichia coli Methionine Aminopeptidase with the Fe(II)-Form Selectivity and Antibacterial Activity †Catalysis and Inhibition of Mycobacterium tuberculosis Methionine AminopeptidaseInhibition of Mycobacterium tuberculosis Methionine Aminopeptidases by Bengamide DerivativesStructural Analysis of Bengamide Derivatives as Inhibitors of Methionine AminopeptidasesPyridinylpyrimidines selectively inhibit human methionine aminopeptidase-1Pyridinylquinazolines Selectively Inhibit Human Methionine Aminopeptidase-1 in CellsHydroxamic acids as potent inhibitors of Fe(II) and Mn(II) E. coli methionine aminopeptidase: biological activities and X-ray structures of oxazole hydroxamate-EcMetAP-Mn complexesAmino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases.Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo.Expression and characterization of Mycobacterium tuberculosis methionine aminopeptidase type 1aAdvances in Bacterial Methionine Aminopeptidase InhibitionDirect genetic selection of two classes of R17/MS2 coat proteins with altered capsid assembly properties and expanded RNA-binding activities.Growth inhibition of Escherichia coli and methicillin-resistant Staphylococcus aureus by targeting cellular methionine aminopeptidase.Development and validation of a whole-cell inhibition assay for bacterial methionine aminopeptidase by surface-enhanced laser desorption ionization-time of flight mass spectrometrySpx mediates oxidative stress regulation of the methionine sulfoxide reductases operon in Bacillus subtilisAnalysis of the stoichiometric metal activation of methionine aminopeptidase.Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases.A cell-based assay that targets methionine aminopeptidase in a physiologically relevant environmentPeptide deformylase as a target for new generation, broad spectrum antimicrobial agents.Amino-terminal extension present in the methionine aminopeptidase type 1c of Mycobacterium tuberculosis is indispensible for its activity.Transcriptional pattern of genes coding for the proteolytic system of Lactococcus lactis and evidence for coordinated regulation of key enzymes by peptide supply.Mutations at the S1 sites of methionine aminopeptidases from Escherichia coli and Homo sapiens reveal the residues critical for substrate specificity.Control of protein life-span by N-terminal methionine excisionStructural basis of catalysis by monometalated methionine aminopeptidaseBridging of a substrate between cyclodextrin and an enzyme's active site pocket triggers a unique mode of inhibitionTwo methionine aminopeptidases from Acinetobacter baumannii are functional enzymes.Methionine aminopeptidases from Mycobacterium tuberculosis as novel antimycobacterial targetsCharacterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA(fMet) formyltransferase.Structural analysis of inhibition of Mycobacterium tuberculosis methionine aminopeptidase by bengamide derivatives.Genetic map of Salmonella typhimurium, edition VIII.Expression, crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Xanthomonas oryzae pv. oryzaeMutation of H63 and its catalytic affect on the methionine aminopeptidase from Escherichia coli.Analyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli.Kinetic and spectroscopic analysis of the catalytic role of H79 in the methionine aminopeptidase from Escherichia coli.Metal-mediated inhibition is a viable approach for inhibiting cellular methionine aminopeptidase.
P2860
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P2860
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
pepM is an essential gene in Salmonella typhimurium.
@ast
pepM is an essential gene in Salmonella typhimurium.
@en
type
label
pepM is an essential gene in Salmonella typhimurium.
@ast
pepM is an essential gene in Salmonella typhimurium.
@en
prefLabel
pepM is an essential gene in Salmonella typhimurium.
@ast
pepM is an essential gene in Salmonella typhimurium.
@en
P2093
P2860
P1476
pepM is an essential gene in Salmonella typhimurium.
@en
P2093
A M Kukral
C G Miller
J L Miller
P2860
P304
P356
10.1128/JB.171.9.5215-5217.1989
P407
P577
1989-09-01T00:00:00Z