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Báo cáo khoa học: Analyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli
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An active site aspartate residue, Asp97, in the methionine aminopeptidase (MetAPs) from Escherichia coli(EcMetAP-I) was mutated to alanine, glu-tamate, and asparagine. Asp97 is the lone carboxylate residue bound to the crystallographically determined second metal-binding site in EcMetAP-I.
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