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The sulfonium functional group present in S-adenosyl methionine is the center of its peculiar reactivity. ... (400–1000 mg). The half-life is about 100 minutes.
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.
The two substrates of this enzyme are S-adenosyl methionine and magnesium protoporphyrin IX; its two products are S-adenosylhomocysteine and magnesium protoporphyrin IX 13-methyl ester. This enzyme belongs to the family of transferases , specifically those transferring one-carbon group methyltransferases.
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).
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-Adenosylmethioninamine is a substrate that is required for the biosynthesis of polyamines including spermidine, spermine, and thermospermine. [1] It is produced by decarboxylation of S -adenosyl methionine .
The systematic name of this enzyme class is S-adenosyl-L-methionine hydrolase. Other names in common use include S-adenosylmethionine cleaving enzyme , methylmethionine-sulfonium-salt hydrolase , and adenosylmethionine lyase .
The enzyme adenosylmethionine decarboxylase (EC 4.1.1.50) catalyzes the conversion of S-adenosyl methionine to S-adenosylmethioninamine. Polyamines such as spermidine and spermine are essential for cellular growth under most conditions, being implicated in many cellular processes including DNA, RNA and protein synthesis.
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