有哪些信誉好的足球投注网站critical factors governing the difference in antizyme-binding affinities between human ornithine decarboxylase and antizyme inhibitor管理关键因素的差异antizyme-binding人类鸟氨酸脱羧酶和antizyme抑制剂之间的亲和力.pdfVIP
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critical factors governing the difference in antizyme-binding affinities between human ornithine decarboxylase and antizyme inhibitor管理关键因素的差异antizyme-binding人类鸟氨酸脱羧酶和antizyme抑制剂之间的亲和力
Critical Factors Governing the Difference in Antizyme- Binding Affinities between Human Ornithine Decarboxylase and Antizyme Inhibitor 1 1,2 1 2 1 Yen-Chin Liu , Yi-Liang Liu , Jia-Yang Su , Guang-Yaw Liu *, Hui-Chih Hung * 1 Department of Life Sciences and Institute of Genomics and Bioinformatics, National Chung-Hsing University, Taichung, Taiwan, 2 Division of Allergy, Immunology and Rheumatology and Institute of Immunology, Chung-Shan Medical University and Hospital, Taichung, Taiwan Abstract Both ornithine decarboxylase (ODC) and its regulatory protein, antizyme inhibitor (AZI), can bind with antizyme (AZ), but the latter has a higher AZ-binding affinity. The results of this study clearly identify the critical amino acid residues governing the difference in AZ-binding affinities between human ODC and AZI. Inhibition experiments using a series of ODC mutants suggested that residues 125 and 140 may be the key residues responsible for the differential AZ-binding affinities. The ODC_N125K/M140K double mutant demonstrated a significant inhibition by AZ, and the IC50 value of this mutant was 0.08 mM, three-fold smaller than that of ODC_WT. Furthermore, the activity of the AZ-inhibited ODC_N125K/M140K enzyme was hardly rescued by AZI. The dissociation constant (K ) of the [ODC_N125K/M140K]-AZ heterodimer was approximately d 0.02 mM, which is smaller than that of WT_ODC by approximately 10-fold and is very close to the Kd value of AZI_WT, suggesting that ODC_N125K/M140K has an AZ-binding affinity higher than that of ODC_WT and similar to that of AZI. The efficiency of the AZI_K125N/K140M double mutant
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