Kumar S, Cheng X, Klimasauskas S, Mi S, Posfai J, Roberts R J, Wilson G G
New England Biolabs, Beverly, MA 01915.
Nucleic Acids Res. 1994 Jan 11;22(1):1-10. doi: 10.1093/nar/22.1.1.
The m5C-MTases form a closely-knit family of enzymes in which common amino acid sequence motifs almost certainly translate into common structural and functional elements. These common elements are located predominantly in a single structural domain that performs the chemistry of the reaction. Sequence-specific DNA recognition is accomplished by a separate domain that contains recognition elements not seen in other structures. This, combined with the novel and unexpected mechanistic feature of trapping a base out of the DNA helix, makes the m5C-MTases an intriguing class of enzymes for further study. The reaction pathway has suddenly become more complicated because of the base-flipping and much remains to be learned about the DNA recognition elements in the family members for which structural information is not yet available.
5-甲基胞嘧啶甲基转移酶（m5C-MTases）构成了一个紧密相关的酶家族，其中常见的氨基酸序列基序几乎肯定会转化为共同的结构和功能元件。这些共同元件主要位于一个执行反应化学过程的单一结构域中。序列特异性DNA识别是由一个单独的结构域完成的，该结构域包含在其他结构中未见的识别元件。这一点，再加上将一个碱基从DNA螺旋中捕获出来这一新颖且意想不到的机制特征，使得m5C-MTases成为一类值得进一步研究的有趣酶。由于碱基翻转，反应途径突然变得更加复杂，而且对于尚未获得结构信息的家族成员中的DNA识别元件，仍有许多有待了解的地方。
