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Kinetic properties and the effect of substrate analogues on 5'-methylthioadenosine nucleosidase from Escherichia coli.

作者信息

Ferro A J, Barrett A, Shapiro S K

出版信息

Biochim Biophys Acta. 1976 Jul 8;438(2):487-94. doi: 10.1016/0005-2744(76)90264-3.

DOI:10.1016/0005-2744(76)90264-3
PMID:782530
Abstract

5'-Methylthioadenosine nucleosidase (EC 3.2.2-) from Escherichia coli has been purified 220-fold. A molecular weight of 31 000 for the enzyme was estimated from gel filtration on Sephadex G-150. The Km for 5'-methylthioadenosine was 3.1-10(-7) M. In addition to 5'-methylthioadenosine, the nucleoside analogues 5'-ethylthioadenosine, 5'-n-propylthioadenosine, and S-adenosyl-homocysteine also served as substrates for the enzyme. These substrate analogues acted as competitive inhibitors of the reaction with 5'-methylthioadenosine. The Ki values for 5'-ethylthioadenosine, 5'-n-propylthioadenosine, and S-adenosylhomocysteine were determined to be 1.3-10(-7) M, 4.6-10(-8) M, and 1.92-10(-7) M respectively.

摘要

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