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学科主题: 药学
题名:
Copper ions inactivate S-adenosylhomocysteine hydrolase
作者: Chen, JJ; Liu, QY; Yang, XD; Wang, K
关键词: copper ; S-adenosyl-L-homocysteine hydrolase ; biological transmethlation
刊名: CHINESE SCIENCE BULLETIN
发表日期: 2002-07-01
卷: 47, 期:14, 页:1176-1179
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Multidisciplinary Sciences
研究领域[WOS]: Science & Technology - Other Topics
关键词[WOS]: MECHANISM ; BINDING ; LIVER ; HOMOCYSTEINE ; ADENOSINE ; KINETICS
英文摘要:

S-adenosylhomocysteine (AdoHcy) hydrolase is an enzyme that regulates biomethylation and some other physiological processes. Recombinant AdoHcy hydrolase was overexpressed in E. coli JM109 and. purified with ion exchange and gel filtration chromatographies. The effects of copper ions (Cu2+) on the activity of AdoHey hydrolase were investigated and the results showed that Cu2+ inhibited the enzyme′s activity by a concentration and time-dependent process. The inhibition constant (K-i) and the apparent rate constant (k(app)) were calculated to be (14 +/- 4) nmol (.) L-1 and (1.08 +/- 0.15) min(-1), respectively. The existence of the natural substrate Ado could to some extent prevent Cu2+ from inactivating the enzyme, suggesting that copper ions possibly could compete with the natural substrate on enzyme′s substrate binding site. Further studies on the mechanism of inhibition are being carried out.

语种: 英语
WOS记录号: WOS:000176841000008
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.bjmu.edu.cn/handle/400002259/55266
Appears in Collections:北京大学药学院_化学生物学系_期刊论文

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作者单位: 1.Peking Univ, Sch Pharmaceut Sci, Dept Biol Chem, Beijing 100083, Peoples R China
2.Peking Univ, Natl Res Labs Nat & Biomimet Drugs, Beijing 100083, Peoples R China

Recommended Citation:
Chen, JJ,Liu, QY,Yang, XD,et al. Copper ions inactivate S-adenosylhomocysteine hydrolase[J]. CHINESE SCIENCE BULLETIN,2002,47(14):1176-1179.
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