Journal
REJUVENATION RESEARCH
Volume 13, Issue 2-3, Pages 362-364Publisher
MARY ANN LIEBERT INC
DOI: 10.1089/rej.2009.0956
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM026020, R37GM026020] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE ON AGING [R21AG032303, R01AG018000, P30AG028748] Funding Source: NIH RePORTER
- NIA NIH HHS [R21 AG032303, AG 032303, P30-AG028748, R01 AG018000, P30 AG028748-04, P30 AG028748] Funding Source: Medline
- NIGMS NIH HHS [R37 GM026020, R01 GM026020] Funding Source: Medline
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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.
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