S adenosyl methionine (SAM)

Amino acid metabolism Lecture on S adenosyl methionine (SAM)
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S-Adenosyl methionine (ademetionine, AdoMet, SAM, SAMe, SAM-e) is a common cosubstrate involved in methyl group transfers. SAM was first discovered in Italy by G. L. Cantoni in 1952.[1] It is made from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase (EC 2.5.1.6). Transmethylation, transsulfuration, and aminopropylation are the metabolic pathways that use SAM. Although these anabolic reactions occur throughout the body, most SAM is produced and consumed in the liver.[1]
The methyl group (CH3) attached to the methionine sulfur atom in SAM is chemically reactive. This allows donation of this group to an acceptor substrate in transmethylation reactions. More than 40 metabolic reactions involve the transfer of a methyl group from SAM to various substrates, such as nucleic acids, proteins, lipids and secondary metabolites.
In bacteria, SAM is bound by the SAM riboswitch, which regulates genes involved in methionine or cysteine biosynthesis. Source of the article published in description is Wikipedia. I am sharing their material. © by original content developers of Wikipedia.
Link- en.wikipedia.org/wiki/Main_Page

[@hosalah170]

well for those who say that your accent is not good i'm actually american and i undertsand every single word so thank you

[@UWzorf]

I think there may be a mistake on the structure of SAH. I believe that there methyl group should have been transferred and the sulphur has lost its charge. I believe that the current structure is that of SAM.

[@rabeaahsan2070]

can u tell me why type 1 restriction enzymes need it for their activity

[@camdendriggers4328]

You have a mistake on your first slide. ATP does not have a sulfur atom, replace H2S with a carbon atom.

[@babybeauty1266]

Sir plz make a hindi video

[@hema11901]

Nice

[@shomusbiologyofficial]

Thank you

[@drmanishee]

nice video

[@sudddubhadani8802]

In Hindi please