Department of Chemistry and Biochemistry , Molecular Biology Institute, University of California , Los Angeles, Los Angeles, California 90095-1569, USA.
Rejuvenation Res. 2010 Apr-Jun;13(2-3):362-4. doi: 10.1089/rej.2009.0956.
The biological methyl donor S-adenosyl-L-methionine [(S,S)-AdoMet] can spontaneously break down under physiological conditions to form the inactive diastereomer (R,S)-AdoMet, which may interfere with cell function. Although several lower organisms metabolize (R,S)-AdoMet via homocysteine methyltransferases, it is unclear how mammals deal with it. In this paper, we show that the mouse liver extracts, containing the BHMT-2 homocysteine methyltransferase candidate for a similar activity, recognizes (S,S)-AdoMet but not (R,S)-AdoMet. We find no evidence for the enzymatic breakdown of (R,S)-AdoMet in these extracts. Thus, mammals may metabolize (R,S)-AdoMet using a different strategy than other organisms.
生物甲基供体 S-腺苷-L-甲硫氨酸 [(S,S)-AdoMet] 在生理条件下可自发分解形成无活性的差向异构体 (R,S)-AdoMet,这可能会干扰细胞功能。尽管几种低等生物可以通过同型半胱氨酸甲基转移酶代谢 (R,S)-AdoMet,但哺乳动物如何处理它尚不清楚。在本文中,我们表明,含有类似活性的 BHMT-2 同型半胱氨酸甲基转移酶候选物的小鼠肝提取物可识别 (S,S)-AdoMet 但不识别 (R,S)-AdoMet。我们在这些提取物中没有发现 (R,S)-AdoMet 酶促分解的证据。因此,与其他生物体相比,哺乳动物可能使用不同的策略来代谢 (R,S)-AdoMet。