大肠杆菌核酸内切酶III和T4紫外线核酸内切酶（核酸内切酶V）在脱嘌呤嘧啶位点的作用机制。
The mechanisms of action of E. coli endonuclease III and T4 UV endonuclease (endonuclease V) at AP sites.
作者信息
Kim J, Linn S
机构信息
Department of Biochemistry, University of California, Berkeley 94720.
出版信息
Nucleic Acids Res. 1988 Feb 11;16(3):1135-41. doi: 10.1093/nar/16.3.1135.
Abstract
Treatment of DNA containing AP sites with either T4 UV endonuclease or with E. coli endonuclease III followed by a human class II AP endonuclease releases a putative beta-elimination product. This result suggests that both the T4 endonuclease and E. coli endonuclease III class I AP endonucleases catalyze phosphodiester bond cleavage via a lyase- rather than a hydrolase mechanism. Indeed, we have not detected a class I AP endonuclease which hydrolytically catalyzes phosphodiester bond cleavage. Whereas these enzymes use a lyase-like rather than a hydrolytic mechanism, they nonetheless catalyze phosphodiester bond cleavage. We suggest that the term endonuclease can be properly applied to them.
摘要
用T4紫外线内切核酸酶或大肠杆菌内切核酸酶III处理含有脱嘌呤嘧啶（AP）位点的DNA，随后用人II类AP内切核酸酶处理，会释放出一种假定的β-消除产物。这一结果表明，T4内切核酸酶和大肠杆菌内切核酸酶III这两种I类AP内切核酸酶都是通过裂合酶而非水解酶机制催化磷酸二酯键的断裂。事实上，我们尚未检测到能水解催化磷酸二酯键断裂的I类AP内切核酸酶。尽管这些酶采用类似裂合酶的而非水解的机制，但它们仍然催化磷酸二酯键的断裂。我们认为内切核酸酶这个术语可以恰当地应用于它们。
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