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Báo cáo Y học: Insights into the reaction mechanism of Escherichia coli agmatinase by site-directed mutagenesis and molecular modelling
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Upon mutation of Asp153 by asparagine, the catalytic activity of agmatinase (agmatine ureohydrolase, EC 3.5.3.11)fromEscherichia coliwas reduced to about 5% of wild-type activity. Tryptophan emission fluorescence (kmax ¼340 nm), and CD spectra were nearly identical for wild-type and D153N agmatinases. TheKmvalue for agmatine (1.6 ± 0.1 mM),aswellastheKi for putrescine inhibition (12 ± 2 mM)and the interaction of the enzyme with the requiredmetal ion,werealsonot alteredbymutation.
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