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S-Adenosyl-L-homocysteine (SAH) is the biosynthetic precursor to homocysteine. [1] SAH is formed by the demethylation of S -adenosyl- L -methionine . [ 2 ] [ 3 ] Adenosylhomocysteinase converts SAH into homocysteine and adenosine .
Adenosylhomocysteinase (EC 3.13.2.1, S-adenosylhomocysteine synthase, S-adenosylhomocysteine hydrolase, adenosylhomocysteine hydrolase, S-adenosylhomocysteinase, SAHase, AdoHcyase) is an enzyme that catalyzes the nicotinamide adenine dinucleotide (NAD +) dependent, reversible hydrolysis of S-adenosylhomocysteine to homocysteine and adenosine.
SAH riboswitches are a kind of riboswitch that bind S-adenosylhomocysteine (SAH). [1] When the coenzyme S-adenosylmethionine (SAM) is used in a methylation reaction, SAH is produced. SAH riboswitches typically up-regulate genes involved in recycling SAH to create more SAM (or the metabolically related methionine ).
The SAM–SAH riboswitch is a conserved RNA structure in certain bacteria that binds S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH) and is therefore presumed to be a riboswitch. [1] SAM–SAH riboswitches do not share any apparent structural resemblance to known riboswitches that bind SAM or SAH.
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SAH riboswitches bind S-adenosylhomocysteine to regulate genes involved in recycling this metabolite that is produced when S-adenosylmethionine is used in methylation reactions. SAM riboswitches bind S-adenosyl methionine (SAM) to regulate methionine and SAM biosynthesis and transport.
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