3493-13-8

Basic information

• Product Name: S-ADENOSYL-L-METHIONINE IODIDE SALT
• Synonyms: SAM-E IODIDE SALT;S-(5'-ADENOSYL)-L-METHIONINE IODIDE;S-ADENOSYL-L-METHIONINE IODIDE SALT;S-ADENOSYLMETHIONINE IODIDE;S-ADENOSYL METHIONINE IODIDE SALT;ADENOSYL-L-METHIONINE, S-IODIDE SALT;S-(5'-deoxy-5'-adenosyl)methionine iodide;S-(5'-Adenosyl)-L-methionine iodide;SAM iodide salt
• CAS NO: 3493-13-8
• Molecular Formula: C₁₅H₂₃N₆O₅S*I
• Molecular Weight: 526.35
• EINECS: 222-486-5
• Product Categories: Nucleic acids
• Mol File: 3493-13-8.mol
• Article Data: 2

Chemical Properties

• Boiling Point: °Cat760mmHg
• Flash Point: °C
• Appearance: /
• Density: g/cm³
• Storage Temp.: −20°C
• Solubility: H2O: 100 mg/mL
• BRN: 4120787
• CAS DataBase Reference: S-ADENOSYL-L-METHIONINE IODIDE SALT(CAS DataBase Reference)
• NIST Chemistry Reference: S-ADENOSYL-L-METHIONINE IODIDE SALT(3493-13-8)
• EPA Substance Registry System: S-ADENOSYL-L-METHIONINE IODIDE SALT(3493-13-8)

Safety Data

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 22-24/25-36-26
• WGK Germany: 3
• F: 8-10-23
• Hazardous Substances Data: 3493-13-8(Hazardous Substances Data)

Usage

Uses

S-(5′-Adenosyl)-L-methionine (SAM, AdoMet) is used as a primary methyl donor molecule in mammalian cell culture and the first step metabolite in methionine biosynthesis.

Biochem/physiol Actions

Methyl donor; cofactor for enzyme-catalyzed methylations, including catechol O-methyltransferase (COMT) and DNA methyltransferases (DNMT). Although present in all cells, it is concentrated in liver where 85% of all methylation reactions occur. It is also involved in regulating liver function, growth, and response to injury.

Upstream product

• 74-88-4 methyl iodide 
• 979-92-0 S-(5'-adenosyl)-L-homocysteine 
• 53276-26-9 (S)-5’-(S)-(3-amino-3-carboxypropyl)-5’-thioadenosine 

Downstream Products

• 721443-68-1 C₂₂H₂₃O₁₂⁽¹⁺⁾ 
• 68795-37-9 peonidin 3-O-glucoside 
• 1391763-81-7 2-(5-hydroxy-1,4-dioxo-1,4-dihydronaphthalen-2-yl)-3-methoxy-5-methylbenzaldehyde 

Relevant articles and documents

Large-scale, protection-free synthesis of Se-adenosyl-l-selenomethionine analogues and their application as cofactor surrogates of methyltransferases

S-Adenosyl-l-methionine (SAM) analogues have previously demonstrated their utility as chemical reporters of methyltransferases. Here we describe the facile, large-scale synthesis of Se-alkyl Se-adenosyl-l-selenomethionine (SeAM) analogues and their precursor, Se-adenosyl-l-selenohomocysteine (SeAH). Comparison of SeAM analogues with their equivalent SAM analogues suggests that sulfonium-to-selenonium substitution can enhance their compatibility with certain protein methyltransferases, favoring otherwise less reactive SAM analogues. Ready access to SeAH therefore enables further application of SeAM analogues as chemical reporters of diverse methyltransferases.