Weight | 399.453 g/mol |
---|---|
Formula | C15H23N6O5S+ |
Hydrogen Acceptors | 10 |
Hydrogen Donors | 4 |
Aromatic Rings | 2 |
Rotatable Bonds | 7 |
S-adenosyl-L-methionine (29908-03-0)
AdoMet · Ademetionine · SAM-e
Score:
#868 in Biochemistry
,
#2322 in Biology
,
#2874 in Chemistry
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- AdoMet-dependent methylation, DNA methyltransferases and base flipping (Nucleic Acids Research, 2001)
- Universal catalytic domain structure of AdoMet-dependent methyltransferases (Journal of Molecular Biology, 1995)
- Purification and cDNA cloning of the AdoMet-binding subunit of the human mRNA (N6-adenosine)-methyltransferase. (RNA, 1997)
- Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet (The EMBO Journal, 2003)
- AdoMet radical proteinsfrom structure to evolutionalignment of divergent protein sequences reveals strong secondary structure element conservation (Nucleic Acids Research, 2004)
- A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine. (Biochemistry, 1993)
-
Including Acute Oral Tox, Skin Sensitization, Eye Irritation, Aquatic Tox, & more. - AdoMet
- Ademetionine
- SAM-e
- S Amet
- FO-1561
- S-Adenosylmethionine
- S Adenosyl L Methionine
- FO 1561
- S Adenosylmethionine
- Samyr
- S-Adenosylmethionine Sulfate Tosylate
- S Adenosylmethionine Sulfate Tosylate
- FO1561
- Gumbaral
-
SMILESC[S+](CCC(C(=O)[O-])[NH3+])CC1C(C(C(O1)N2C=NC3=C2N=CN=C3N)O)O
-
InChIKeyMEFKEPWMEQBLKI-UHFFFAOYSA-O
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