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Low Temperature Induced Conformation Changes of Aminoacylase
作者姓名:谢强  孟凡国  周海梦
作者单位:Department of Biological Sciences and Biotechnology,Tsinghua University,Beijing 100084,Department of Biological Sciences and Biotechnology,Tsinghua University,Beijing 100084,Department of Biological Sciences and Biotechnology,Tsinghua University,Beijing 100084,China,Protein Science Laboratory of the Ministry of Education,School of Life Science and Engineering,Tsinghua University,Beijing 100084,China
基金项目:the National Key Basic Research and Development (973) Program of China (No. G1999075607)
摘    要:Introduction Aminoacylase (N-acylamino acid amido hydrolase. EC 3.5.1.14), which exists in mammalian kidneys and microorganisms, catalyzes the reversible hydrolysis of L-acylamino acids1]. The enzyme is dimeric with a relative molecular mass of 8.6?04, containing one Zn2 ion per subunit, which is essential for enzyme activity2,3]. The two subunits of the enzyme are identical in sequence. Although the primary structure of aminoacylase has been determined by cDNA sequencing4,5], no X-ray…


Low Temperature Induced Conformation Changes of Aminoacylase
XIE Qiang ,MENG Fanguo.Low Temperature Induced Conformation Changes of Aminoacylase[J].Tsinghua Science and Technology,2004,9(1).
Authors:XIE Qiang  MENG Fanguo
Institution:XIE Qiang 1,MENG Fanguo
Abstract:
Keywords:low temperature  aminoacylase  secondary structure
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