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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). [1]
Radical SAM enzymes belong to a superfamily of enzymes that use an iron-sulfur cluster to reductively cleave S-adenosyl-L-methionine (SAM) to generate a radical, usually a 5′-deoxyadenosyl radical (5'-dAdo), as a critical intermediate.
S-adenosylmethionine-dependent methyltransferase (SAM-MTase or AdoMet-MTase) is a conserved protein domain and protein superfamily. [1] SAM-MTase proteins are methyltransferases. [2] There are five protein families within SAM-MTase, SAM-MTases use S-adenosyl-L-methionine as a substrate for methylation, creating the product S-adenosyl-L ...
8-hydroxyfuranocoumarin 8-O-methyltransferase (EC 2.1.1.70, furanocoumarin 8-methyltransferase, furanocoumarin 8-O-methyl-transferase, xanthotoxol 8-O-methyltransferase, XMT, SAM:xanthotoxol O-methyltransferase, S-adenosyl-L-methionine:8-hydroxyfuranocoumarin 8-O-methyltransferase, xanthotoxol methyltransferase, xanthotoxol O-methyltransferase, S-adenosyl-L-methionine:xanthotoxol O ...
Lipoyl synthase is an enzyme that belongs to the radical SAM (S-adenosyl methionine) family. Within the radical SAM superfamily, lipoyl synthase is in a sub-family of enzymes that catalyze sulfur insertion reactions. The enzymes in this subfamily differ from general radical SAM enzymes, as they contain two 4Fe-4S clusters.
S-adenosyl methionine (SAM) is the precursor to 5′-methylthioadenosine. The pervasive cofactor S-adenosyl methionine (SAM) is the precursor to 5′-methylthioadenosine. The sulfonium group in SAM can cleave in three ways, one involves loss of CH 2 CH 2 CH(NH 3 +)CO 2 −, generating the title compound.
Radical S-adenosylmethionine enzymes, otherwise known as radical SAM enzymes, are metalloproteins that cleave S-adenosyl-L-methionine into L-methionine and a 5'-deoxyadenosyl 5'-radical (5'-dA). [ 3 ] 5'-dA is an intermediate in the reactions catalyzed by radical SAMs. 5'-dA removes a hydrogen from the substrate and allows for the addition of ...
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