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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.
16S rRNA (guanine 527-N 7)-methyltransferase (EC 2.1.1.170, ribosomal RNA small subunit methyltransferase G, 16S rRNA methyltransferase RsmG, GidB, rsmG (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (guanine 527-N 7)-methyltransferase. [1] [2] This enzyme catalyses the following chemical reaction
Methyl halide transferase (EC 2.1.1.165, MCT, methyl chloride transferase, S-adenosyl-L-methionine:halide/bisulfide methyltransferase, AtHOL1, AtHOL2, AtHOL3, HMT, S-adenosyl-L-methionine: halide ion methyltransferase, SAM:halide ion methyltransferase) is an enzyme with systematic name S-adenosylmethionine:iodide methyltransferase.
16S rRNA (cytosine 1402-N 4)-methyltransferase (EC 2.1.1.199, RsmH, MraW) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytosine1402-N4)-methyltransferase. [1] This enzyme catalyses the following chemical reaction
2 S-adenosyl-L-methionine + adenine 2085 in 23S rRNA 2 S-adenosyl-L-homocysteine + N 6-dimethyladenine 2085 in 23S rRNA. ErmC is a methyltransferase that confers resistance to the macrolide-lincosamide-streptogramin B group of antibiotics by catalysing the methylation of 23S rRNA at adenine 2085.
Thus, the two substrates of this enzyme are S-adenosyl-L-methionine and H 2 O, whereas its two products are L-homoserine and methylthioadenosine. This enzyme belongs to the family of hydrolases , specifically those acting on ether bonds involving sulfur (thioether and trialkylsulfonium hydrolases).
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