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学科主题药学
Binding of Cu2+ to S-adenosyl-L-homocysteine hydrolase
Li, YJ; Chen, JJ; Liu, J; Yang, XD; Wang, K
关键词copper S-Adenosyl-L-homocysteine hydrolase kinetic
刊名JOURNAL OF INORGANIC BIOCHEMISTRY
2004-06-01
DOI10.1016/j.jinorgbio.2004.02.013
98期:6页:977-983
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Biochemistry & Molecular Biology ; Chemistry, Inorganic & Nuclear
研究领域[WOS]Biochemistry & Molecular Biology ; Chemistry
关键词[WOS]ADENOSYLHOMOCYSTEINE HYDROLASE ; COPPER-BINDING ; MECHANISM ; PROTEIN ; LIVER ; INACTIVATION ; KINETICS ; IONS
英文摘要

S-Adenosylhomocysteine (AdoHcy) hydrolase regulates biomethylation and homocysteine metabolism. It has been proposed to be a copper binding protein playing an important role in copper transport and distribution. In the present work, the kinetics of binding and releasing of copper ions was studied using fluorescence method. The dissociation constant for copper ions with AdoHcy hydrolase was determined by fluorescence quenching titration and activity titration methods using ethylenediaminetetra acetic acid (EDTA), nitrilotriacetic acid (NTA), and glycine as competitive chelators. The experimental results showed that copper ions bind to AdoHcy hydrolase with a K-d of similar to 10(-11) M. The association rate constant was determined to be 7 x 10(6) M-1 s(-1). The releasing of copper ions from the enzyme was found to be biphasic with a k((1)) of 2.8 x 10(-3) s(-1) and k(2) of 1.7 x 10(-5) s(-1). It is suggested that copper ions do not bind to the substrate binding sites because the addition of adenine substrate did not compete with the binding of copper to AdoHcy hydrolase. Interestingly, it was observed that EDTA could bind to AdoHcy hydrolase with a dissociation constant of K-1 = 8.0 x 10(-5) M and result in an increased affinity (K-d = similar to 10(-17) M) of binding of copper ions to the enzyme. (C) 2004 Elsevier Inc. All rights reserved.

语种英语
WOS记录号WOS:000221939000008
Citation statistics
Cited Times:8[WOS]   [WOS Record]     [Related Records in WOS]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/62842
Collection北京大学药学院_化学生物学系
作者单位1.Peking Univ, Hlth Sci Ctr, Sch Pharmaceut Sci, Dept Biol Chem, Beijing 100083, Peoples R China
2.Peking Univ, Hlth Sci Ctr, Natl Res Labs Nat & Biomimet Drugs, Beijing 100083, Peoples R China
Recommended Citation
GB/T 7714
Li, YJ,Chen, JJ,Liu, J,et al. Binding of Cu2+ to S-adenosyl-L-homocysteine hydrolase[J]. JOURNAL OF INORGANIC BIOCHEMISTRY,2004,98(6):977-983.
APA Li, YJ,Chen, JJ,Liu, J,Yang, XD,&Wang, K.(2004).Binding of Cu2+ to S-adenosyl-L-homocysteine hydrolase.JOURNAL OF INORGANIC BIOCHEMISTRY,98(6),977-983.
MLA Li, YJ,et al."Binding of Cu2+ to S-adenosyl-L-homocysteine hydrolase".JOURNAL OF INORGANIC BIOCHEMISTRY 98.6(2004):977-983.
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