Structural Insights into the Catalytic Active Site and Activity of Human Nit2/ω-Amidase KINETIC ASSAY AND MOLECULAR DYNAMICS SIMULATION

CH Chien, QZ Gao, AJL Cooper, JH Lyu…

文献索引：Chien, Chin-Hsiang; Gao, Quan-Ze; Cooper, Arthur J. L.; Lyu, Jyun-Hong; Sheu, Sheh-Yi Journal of Biological Chemistry, 2012 , vol. 287, # 31 p. 25715 - 25726

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被引用次数: 7

摘要

Results: Both the catalytic triad and loop 116–128 of hNit2 play an essential role in the enzyme-substrate binding and enzymatic activity. Conclusion: The results of MD simulations are consistent with the kinetic analysis obtained with substrates α-ketoglutaramate and succinamate.