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一种来自大肠杆菌的N-糖苷酶,可从含有脱氨基胞嘧啶残基的DNA中释放游离尿嘧啶。

An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues.

作者信息

Lindahl T

出版信息

Proc Natl Acad Sci U S A. 1974 Sep;71(9):3649-53. doi: 10.1073/pnas.71.9.3649.

Abstract

An enzyme that liberates uracil from single-stranded and double-stranded DNA containing deaminated cytosine residues and from deoxycytidylate-deoxyuridylate copolymers in the absence of Mg(++) has been purified 30-fold from cell extracts of E. coli. The enzyme does not release uracil from deoxyuridine, dUMP, uridine, or RNA, nor does it liberate the normally occurring pyrimidine bases, cytosine and thymine, from DNA. The enzymatic cleavage of N-glycosidic bonds in DNA occurs without concomitant cleavage of phosphodiester bonds, resulting in the formation of free uracil and DNA strands of unaltered chain length that contain apyrimidinic sites as reaction products. The enzyme may be active in DNA repair, converting deaminated dCMP residues to an easily repairable form.

摘要

一种能在无Mg(++)的情况下,从含有脱氨基胞嘧啶残基的单链和双链DNA以及脱氧胞苷酸-脱氧尿苷酸共聚物中释放尿嘧啶的酶,已从大肠杆菌细胞提取物中纯化了30倍。该酶不会从脱氧尿苷、dUMP、尿苷或RNA中释放尿嘧啶,也不会从DNA中释放正常存在的嘧啶碱基胞嘧啶和胸腺嘧啶。DNA中N-糖苷键的酶促切割过程中不会伴随磷酸二酯键的切割,从而形成游离尿嘧啶和链长不变但含有脱嘧啶位点的DNA链作为反应产物。该酶可能在DNA修复中发挥作用,将脱氨基的dCMP残基转化为易于修复的形式。

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