S-Adenosyl methionine is a common cosubstrate involved in methyl group transfers, transsulfuration, and aminopropylation.

S-Adenosyl methionine can subsequently methylate the amine of phosphatidylethanolamines to yield phosphatidylcholines.

Some of the amino acid substrates become N-methylated by S-Adenosyl methionine.

A small amount of compound 5 can be isolated, however S-Adenosyl methionine methylates most of it and gives yangonin 6.

The authors posit that the flanking amino acid groups are probably derived biosynthetically from S-Adenosyl methionine.

He pioneered the therapeutic use of the coenzyme S-Adenosyl methionine as a therapeutic means to prevent liver toxicity.

S-Adenosyl methionine (SAM) can act as a catalyst for the transfer of methyl group from the sulfonium compound to nucleophile.

S-Adenosyl methionine (SAMe) is available as a prescription antidepressant in Europe and an over-the-counter dietary supplement in the US.

In both types of histone methyltransferases, cofactor S-Adenosyl methionine (SAM) serves as a cofactor and methyl donor group.

Histone methyltransferases are enzymes which transfer methyl groups from S-Adenosyl methionine onto the lysine or arginine residues of the H3 and H4 histones.

The most common class of methyltransferases is class I, all of which contain a Rossman fold for binding S-Adenosyl methionine (SAM).

It accomplishes this interconversion using three cofactors and a 5'-deoxyadenosyl radical formed in a S-Adenosyl methionine (SAM) activated radical reaction pathway.

Each MetJ dimer contains two binding sites for the cofactor S-Adenosyl methionine (SAM) which is a product in the biosynthesis of methionine.

Imine exchange An imine exchange occurs, and the amine nitrogen of the substrate, S-Adenosyl methionine, replaces Lys (278) in the imine linkage.

Recent work has revealed the methyltransferases involved in methylation of naturally-occurring anticancer agents to use S-Adenosyl methionine (SAM) analogs that carry alternative alkyl groups as a replacement for methyl.

The adenosyl and methionine main-chain moieties of S-Adenosyl methionine (SAM) are recognized through hydrogen-bonding into the bulge in P3 and the conserved G in J1/2.

Methionine synthase's main purpose is to regenerate Met in the S-Adenosyl Methionine cycle, which in a single turnover consumes Met and ATP and generates Hcy.

The activity of Fe-ARD is closely interwoven with the methionine salvage pathway, in which the methylthioadenosine product of cellular S-Adenosyl methionine (SAM) reactions is eventually converted to acireductone.

In order for the reaction to proceed, S-Adenosyl methionine (SAM) and the lysine residue of the substrate histone tail must first be bound and properly oriented in the catalytic pocket of the SET domain.

Radical SAM is a designation for group of enzymatic reactions sharing the property that an iron-sulfur cluster in the enzyme cleaves S-Adenosyl methionine (SAM) reductively to produce a radical, usually a 5'-deoxyadenosyl radical, as a critical intermediate.

Both choline and folate (with the help of vitamin B) can act as methyl donors to homocysteine to form methionine, which can then go on to form SAM (S-Adenosyl methionine) and act as a methyl donor for methylation of DNA.

The Anaerobic Enzymology bridging project will explore radical-dependent enzymology, which allows the execution of unusual chemical transformations via an iron-sulfur cluster cleaving S-Adenosyl methionine (SAM) and producing a radical intermediate, or alternatively, abstraction of a hydrogen from glycine producing a glycyl radical.