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Glu395 is directly interacting with amino group of the inhibitor
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competitive inhibitor, the inhibitory effect is fully reversed by SSAM substrate benzamide, demonstrating the hydrophobicity of the active site
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the inhibitor is able to thoroughly protect the flap cysteines from the further reaction with disulfides, this apparently resulting from the closed conformation of the flap. The inhibitor may be regarded as the most suitable inhibitor for active-site protection experiments in inhibition studies of urease
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Urethane-hydrolyzing enzyme from Citrobacter sp
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Molecular modeling and docking of wheat hydroquinone glucosyl transferase by using hydroquinone, phenyl phosphorodiamate and n-(n butyl) phosphorothiocic triamide as inhibitors
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Bioinformation
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124-129