Yeast, Plants, Worms, and Flies Use a Methyltransferase to Metabolize Age-Damaged (R,S)-AdoMet, but What Do Mammals Do?

被引：6

作者：

Vinci, Chris R.

Clarke, Steven G. ^{[1
]}

机构：

[1] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA

来源：

REJUVENATION RESEARCH | 2010年 / 13卷 / 2-3期

关键词：

ADENOSYL-L-METHIONINE; S-ADENOSYLMETHIONINE; HOMOCYSTEINE METHYLTRANSFERASE; PROTEIN METHYLATION; SULFONIUM CENTER; BIOLOGY; CONFIGURATION; RECOGNITION; CHEMISTRY; STRUGGLE;

D O I：

10.1089/rej.2009.0956

中图分类号：

R592 [老年病学]; C [社会科学总论];

学科分类号：

03 ; 0303 ; 100203 ;

摘要：

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.

引用

页码：362 / 364

页数：3