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S-Adenosyl methionine (SAM), also known under the commercial names of SAMe, SAM-e, or AdoMet, is a common cosubstrate involved in methyl group transfers, transsulfuration, and aminopropylation. Although these anabolic reactions occur throughout the body, most SAM is produced and consumed in the liver. [ 1 ]
S-Adenosylmethionine synthetase (EC 2.5.1.6), also known as methionine adenosyltransferase (MAT), is an enzyme that creates S-adenosylmethionine (also known as AdoMet, SAM or SAMe) by reacting methionine (a non-polar amino acid) and ATP (the basic currency of energy).
In addition, several non-canonical radical SAM enzymes have been described. These cannot be recognized by the Pfam hidden Markov model PF04055, but still use three Cys residues as ligands to a 4Fe4S cluster and produce a radical from S-adenosylmethionine. These include
Tosyl group (blue) with a generic "R" group attached Tosylate group with a generic "R" group attached. Note the extra oxygen, compared to plain tosyl. In organic chemistry, a toluenesulfonyl group (tosyl group, abbreviated Ts or Tos [nb 1]) is a univalent functional group with the chemical formula −SO 2 −C 6 H 4 −CH 3.
These enzymes use S-adenosylmethionine as a methyl donor and contain several highly conserved structural features between the three forms; these include the S-adenosylmethionine binding site, a vicinal proline-cysteine pair which forms a thiolate anion important for the reaction mechanism, and the cytosine substrate binding pocket.
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S-Adenosylmethionine:tRNA ribosyltransferase-isomerase (EC 2.4.99.17, QueA enzyme, queuosine biosynthesis protein QueA) is an enzyme with systematic name S-adenosyl-L-methionine:7-aminomethyl-7-deazaguanosine ribosyltransferase (ribosyl isomerizing; L-methionine, adenine releasing).
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