Disease relevance of S-adenosylmethionine

• In E. coli MG1655, expression of T3SH [the bacteriophage T3 S-adenosylmethionine (SAM) hydrolase] significantly reduced AI-2 activity in culture supernatants, suggesting that AI-2 production is limited by the amount of SAH produced in SAM-dependent transmethylase reactions [1].

High impact information on S-adenosylmethionine

• Using limited amounts of the methyl donor S-adenosylmethionine (SAM) a partial level of methylation (50% of control) was attained [2].
• Additionally, the cell-free solution also catalyzed the C-24 methylation of 28-norCS to CS in the presence of NADPH and S-adenosylmethionine (SAM), a reaction that was clearly retarded in the absence of NADPH and SAM [3].
• Glycine N-methyltransferase (GNMT) functions to regulate S-adenosylmethionine (SAM) levels and the ratio of SAM/S-adenosylhomocysteine (SAH) [4].
• Therefore, it is concluded that SAM is a methyl donor for 1-MeAde biosynthesis in starfish ovarian follicle cells [5].
• The incubation of 1mM MPP+ and various concentrations of SAM (0-4 mM) decreased the viability of PC12 cells from 80% with MPP+ alone to 38% viability with 4 mM SAM for 4 days incubation [6].

Anatomical context of S-adenosylmethionine

• IL-1 is likely to decrease SAM levels in chondrocytes; supplemental SAM may compensate for this deficit [7].

Associations of S-adenosylmethionine with other chemical compounds

• The hepatic level of the PE methyltransferase co-substrate, S-adenosylmethionine (SAM), decreased about 1/3, but the level of the inhibitory metabolite, S-adenosylhomocysteine (SAH), was elevated due to the marked reduction in the activities of cystathionine beta-synthase and gamma-cystathionase [8].

References