53276-26-9

Basic information

• Product Name: S-(5''-Adenosyl)-D-homocysteine
• Synonyms: S-(5''-Adenosyl)-D-homocysteine;S-adenosyl-D-homocysteine;(2R)-2-Amino-4-[(5'-deoxyadenosine-5'-yl)thio]butanoic acid;5'-S-[(R)-3-Amino-3-carboxypropyl]-5'-thioadenosine;Adenosyl-D-homocysteine;(R)-2-Amino-4-((((2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl;(R)-2-AMino-4-((((2S,3S,4R,5R)-5-(6-aMino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)Methyl)thio)butanoic acid;5′-Deoxy-S-adenosyl-D-homocysteine
• CAS NO: 53276-26-9
• Molecular Formula: C₁₄H₂₀N₆O₅S
• Molecular Weight: 384.42
• Mol File: 53276-26-9.mol
• Article Data: 2

Chemical Properties

• Appearance: /
• Storage Temp.: ?20°C
• CAS DataBase Reference: S-(5''-Adenosyl)-D-homocysteine(CAS DataBase Reference)
• NIST Chemistry Reference: S-(5''-Adenosyl)-D-homocysteine(53276-26-9)
• EPA Substance Registry System: S-(5''-Adenosyl)-D-homocysteine(53276-26-9)

Safety Data

• Hazardous Substances Data: 53276-26-9(Hazardous Substances Data)

Usage

General Description

S-(5'-Adenosyl)-D-homocysteine, also known as adenosylhomocysteine, is a byproduct of various cellular methylation reactions and is a potent inhibitor of S-adenosyl-L-methionine-dependent methyltransferases. It is formed from the methylation of homocysteine by S-adenosyl-L-methionine during the transfer of a methyl group to various biomolecules. Adenosylhomocysteine plays a crucial role in regulating cellular methylation reactions by acting as a feedback inhibitor that can prevent excessive methylation. In addition to its role as an intermediate in methylation reactions, adenosylhomocysteine has also been implicated in promoting inflammation and cell adhesion, making it an important molecule for the regulation of cellular processes. Its dysregulation has been linked to various diseases, including cancer, cardiovascular diseases, and neuropsychiatric disorders.

Upstream product

• 454-28-4 D-homocysteine 
• 5605-63-0 ((3aR,4R,6R,6aR)-6-(6-amino-9H-purin-9-yl)-2,2-dimethyl-tetrahydrofuro[3,4-d][1,3]dioxol-4-yl)methyl 4-methylbenzenesulfonate 
• 892-48-8 5'-deoxy-5'-chloroadenosine 
• 88945-99-7 D-Homocysteine monosodium salt 

Downstream Products

• 3493-13-8 S-adenosyl-L-methionine iodide 

Relevant articles and documents

Radical SAM-Dependent Demetallation of Heme

Demetallation of heme to release iron is a chemical difficult reaction and is highly rare in biochemistry, with apoferritin as the only known enzyme responsible for this process. Here we show the heme degradation enzyme ChuW catalyzes heme demetallation besides its known methyltransferase activity (which converts heme to a ring-open product anaerobilin). We show the demetallation activity of ChuW is radical SAM-dependent, and likely involves the same set of intermediates involved in the anaerobilin-producing pathway. The ChuW-catalyzed demetallation reaction does not require external reductant, and can occur on several heme analogs with different metal centers. These findings establish a brand-new chemistry in the radical SAM enzymes, highlighting the remarkable catalytic diversity of this superfamily of enzymes.