Structural basis of catalysis by monometalated methionine aminopeptidase
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Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movementsInhibition 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 enzymesStructural Basis for Catalysis by the Mono- and Dimetalated Forms of the dapE-Encoded N-succinyl-l,l-Diaminopimelic Acid DesuccinylasePyridinylpyrimidines 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 complexesDetermination of binding affinity of metal cofactor to the active site of methionine aminopeptidase based on quantitation of functional enzymeAnalysis of the stoichiometric metal activation of methionine aminopeptidase.A global investigation of the Bacillus subtilis iron-sparing response identifies major changes in metabolism.Bridging of a substrate between cyclodextrin and an enzyme's active site pocket triggers a unique mode of inhibitionCrystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active siteMutation of H63 and its catalytic affect on the methionine aminopeptidase from Escherichia coli.Analyzing the binding of Co(II)-specific inhibitors to the methionyl aminopeptidases from Escherichia coli and Pyrococcus furiosusAnalyzing 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.Lysine biosynthesis in bacteria: a metallodesuccinylase as a potential antimicrobial target.Magnetic circular dichroism study of a dicobalt(II) complex with mixed 5- and 6-coordination: a spectroscopic model for dicobalt(II) hydrolases.Metal-mediated inhibition is a viable approach for inhibiting cellular methionine aminopeptidase.Motif-directed redesign of enzyme specificity.Probing the metal ion selectivity in methionine aminopeptidase via changes in the luminescence properties of the enzyme bound europium ionFE(II) is the native cofactor for Escherichia coli methionine aminopeptidase.
P2860
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P2860
Structural basis of catalysis by monometalated methionine aminopeptidase
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2006 nî lūn-bûn
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2006 թուականի Յունիսին հրատարակուած գիտական յօդուած
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2006 թվականի հունիսին հրատարակված գիտական հոդված
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2006年の論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
@zh-tw
2006年论文
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name
Structural basis of catalysis by monometalated methionine aminopeptidase
@ast
Structural basis of catalysis by monometalated methionine aminopeptidase
@en
Structural basis of catalysis by monometalated methionine aminopeptidase
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type
label
Structural basis of catalysis by monometalated methionine aminopeptidase
@ast
Structural basis of catalysis by monometalated methionine aminopeptidase
@en
Structural basis of catalysis by monometalated methionine aminopeptidase
@nl
prefLabel
Structural basis of catalysis by monometalated methionine aminopeptidase
@ast
Structural basis of catalysis by monometalated methionine aminopeptidase
@en
Structural basis of catalysis by monometalated methionine aminopeptidase
@nl
P2093
P2860
P356
P1476
Structural basis of catalysis by monometalated methionine aminopeptidase
@en
P2093
Qi-Zhuang Ye
Robert P Hanzlik
Sheng-Xue Xie
Ze-Qiang Ma
P2860
P304
P356
10.1073/PNAS.0602433103
P407
P577
2006-06-12T00:00:00Z