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Record Information
StatusDetected and Quantified
Creation Date2005-11-16 15:48:42 UTC
Update Date2017-12-23 02:53:07 UTC
Secondary Accession Numbers
  • HMDB01185
Metabolite Identification
Common NameS-Adenosylmethionine
DescriptionPhysiologic methyl radical donor involved in enzymatic transmethylation reactions and present in all living organisms. It possesses anti-inflammatory activity and has been used in treatment of chronic liver disease. (From Merck, 11th ed)
(3S)-5'-[(3-amino-3-Carboxypropyl)methylsulfonio]-5'-deoxyadenosine, inner saltChEBI
(3S)-5'-[(3-amino-3-Carboxypropyl)methylsulphonio]-5'-deoxyadenosine, inner saltGenerator
5'-Deoxyadenosine-5'-L-methionine disulfate ditosylateHMDB
5'-Deoxyadenosine-5'-L-methionine disulphate ditosylateHMDB
Active methionineHMDB
S-Adenosyl methionineHMDB
S-Adenosyl-L-methionine disulfate tosylateHMDB
S-Adenosyl-L-methionine disulphate tosylateHMDB
ASTA medica brand OF ademetionine tosilate disulfateMeSH
S Adenosylmethionine sulfate tosylateMeSH
S-Adenosylmethionine sulfate tosylateMeSH
Sulfate tosylate, S-adenosylmethionineMeSH
Ademetionine europharma brandMeSH
Amet, SMeSH
Europharma brand OF ademetionineMeSH
Knoll brand OF brand OF ademetionine tosilate disulfateMeSH
S AdenosylmethionineMeSH
S AmetMeSH
Tosylate, S-adenosylmethionine sulfateMeSH
Chemical FormulaC15H23N6O5S
Average Molecular Weight399.445
Monoisotopic Molecular Weight399.145063566
IUPAC Name[(3S)-3-amino-3-carboxypropyl]({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl})methylsulfanium
Traditional NameSAMe
CAS Registry Number29908-03-0
InChI Identifier
Chemical Taxonomy
DescriptionThis compound belongs to the class of chemical entities known as 5'-deoxy-5'-thionucleosides. These are 5'-deoxyribonucleosides in which the ribose is thio-substituted at the 5'position by a S-alkyl group.
KingdomChemical entities
Super ClassOrganic compounds
ClassNucleosides, nucleotides, and analogues
Sub Class5'-deoxyribonucleosides
Direct Parent5'-deoxy-5'-thionucleosides
Alternative Parents
  • 5'-deoxy-5'-thionucleoside
  • Methionine or derivatives
  • N-glycosyl compound
  • Glycosyl compound
  • 6-aminopurine
  • Alpha-amino acid
  • Alpha-amino acid or derivatives
  • Pentose monosaccharide
  • L-alpha-amino acid
  • Imidazopyrimidine
  • Purine
  • Hydroxy fatty acid
  • Aminopyrimidine
  • Thia fatty acid
  • N-substituted imidazole
  • Monosaccharide
  • Primary aromatic amine
  • Pyrimidine
  • Fatty acyl
  • Imidolactam
  • Heteroaromatic compound
  • Imidazole
  • Azole
  • Oxolane
  • 1,2-diol
  • Amino acid or derivatives
  • Secondary alcohol
  • Amino acid
  • Oxacycle
  • Azacycle
  • Carboxylic acid derivative
  • Carboxylic acid
  • Organoheterocyclic compound
  • Monocarboxylic acid or derivatives
  • Organic oxide
  • Organopnictogen compound
  • Alcohol
  • Carbonyl group
  • Organic oxygen compound
  • Organic nitrogen compound
  • Hydrocarbon derivative
  • Primary amine
  • Organosulfur compound
  • Organooxygen compound
  • Primary aliphatic amine
  • Amine
  • Organonitrogen compound
  • Organic cation
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Physiological effect

Health effect:

  Health condition:


Biological Location:


  Biofluid and excreta:

  Tissue and substructures:

  Organ and components:

  Cell and elements:



Route of exposure:



Naturally occurring process:

  Biological process:

    Biochemical pathway:


Indirect biological role:

Physical Properties
Experimental Properties
Melting PointNot AvailableNot Available
Boiling Point78 °CNot Available
Water Solubility1.19 g/lALOGPS
Predicted Properties
Water Solubility1.19 g/LALOGPS
pKa (Strongest Acidic)1.71ChemAxon
pKa (Strongest Basic)9.41ChemAxon
Physiological Charge1ChemAxon
Hydrogen Acceptor Count10ChemAxon
Hydrogen Donor Count5ChemAxon
Polar Surface Area182.63 ŲChemAxon
Rotatable Bond Count7ChemAxon
Refractivity96.23 m³·mol⁻¹ChemAxon
Polarizability40.37 ųChemAxon
Number of Rings3ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectrum TypeDescriptionSplash Key
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0a5c-5965000000-324e4a3cbf936132bcf1View in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (3 TMS) - 70eV, Positivesplash10-00ea-7958582000-3dd40cf273f182ee53ddView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-0002-0019000000-6dfa0dc65a9863755c2aView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-0udj-0293000000-57cc9d4430592060d41dView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-0udr-1940000000-ed4985bea80649d27efeView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-000b-8920000000-8f05e9898f0d26ddf3f8View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-000e-9400000000-e5c5617045d9915e8e46View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-IT , positivesplash10-0udi-0090000000-93017671648813ece8a5View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000i-0914000000-95030ceaf1c187dcf656View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-0900000000-c3fae8b7a68475b614a4View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-2900000000-44078fd7eaeafcc5bba8View in MoNA
Biological Properties
Cellular Locations
  • Mitochondria
  • Nucleus
  • Endoplasmic reticulum
Biofluid Locations
  • Blood
  • Cerebrospinal Fluid (CSF)
  • Feces
  • Urine
Tissue Location
  • Epidermis
  • Eye Lens
  • Fibroblasts
  • Gonads
  • Intestine
  • Kidney
  • Muscle
  • Myelin
  • Placenta
  • Prostate
  • Skeletal Muscle
  • Testes
3-Phosphoglycerate dehydrogenase deficiencyPw000698Pw000698 greyscalePw000698 simpleNot Available
AlkaptonuriaPw000180Pw000180 greyscalePw000180 simpleNot Available
Arginine and Proline MetabolismPw000010Pw000010 greyscalePw000010 simpleMap00330
Arginine: Glycine Amidinotransferase Deficiency (AGAT Deficiency)Pw000084Pw000084 greyscalePw000084 simpleNot Available
Aromatic L-Aminoacid Decarboxylase DeficiencyPw000090Pw000090 greyscalePw000090 simpleNot Available
Normal Concentrations
Cerebrospinal Fluid (CSF)Detected and Quantified0.25 (0.14 - 0.38) uMAdult (>18 years old)BothNormal details
Abnormal Concentrations
BloodDetected and Quantified0.11 (0.087-0.17) uMAdult (>18 years old)BothNeurodegenerative diseases details
FecesDetected but not Quantified Children (6 - 18 years old)Bothenthesitis-related arthritis details
UrineDetected and Quantified28.4 (25.3-31.6) umol/mmol creatinineAdult (>18 years old)Both
Associated Disorders and Diseases
Disease References
Diabetes mellitus type 2
  1. Hoppel CL, Genuth SM: Urinary excretion of acetylcarnitine during human diabetic and fasting ketosis. Am J Physiol. 1982 Aug;243(2):E168-72. [PubMed:6810706 ]
Neurodegenerative disease
  1. Obeid R, Kostopoulos P, Knapp JP, Kasoha M, Becker G, Fassbender K, Herrmann W: Biomarkers of folate and vitamin B12 are related in blood and cerebrospinal fluid. Clin Chem. 2007 Feb;53(2):326-33. Epub 2007 Jan 2. [PubMed:17200133 ]
Associated OMIM IDs
DrugBank IDDB00118
Phenol Explorer Compound IDNot Available
FoodDB IDFDB022473
KNApSAcK IDC00007347
Chemspider ID21169292
KEGG Compound IDC00019
BiGG ID33530
Wikipedia LinkS-Adenosyl_methionine
PubChem Compound16757548
ChEBI ID15414
Synthesis ReferenceLin, Jian-Ping; Tian, Jun; You, Jian-Feng; Jin, Zhi-Hua; Xu, Zhi-Nan; Cen, Pei-Lin. An effective strategy for the co-production of S-adenosyl-L-methionine and glutathione by fed-batch fermentation. Biochemical Engineering Journal (2004), 21(1), 19-25.
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. Chamberlin ME, Ubagai T, Mudd SH, Wilson WG, Leonard JV, Chou JY: Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency. J Clin Invest. 1996 Aug 15;98(4):1021-7. [PubMed:8770875 ]
  2. Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. doi: 10.1038/nature07762. [PubMed:19212411 ]
  3. Hoppel CL, Genuth SM: Urinary excretion of acetylcarnitine during human diabetic and fasting ketosis. Am J Physiol. 1982 Aug;243(2):E168-72. [PubMed:6810706 ]
  4. Koeberl DD, Young SP, Gregersen NS, Vockley J, Smith WE, Benjamin DK Jr, An Y, Weavil SD, Chaing SH, Bali D, McDonald MT, Kishnani PS, Chen YT, Millington DS: Rare disorders of metabolism with elevated butyryl- and isobutyryl-carnitine detected by tandem mass spectrometry newborn screening. Pediatr Res. 2003 Aug;54(2):219-23. Epub 2003 May 7. [PubMed:12736383 ]
  5. Struys EA, Jansen EE, de Meer K, Jakobs C: Determination of S-adenosylmethionine and S-adenosylhomocysteine in plasma and cerebrospinal fluid by stable-isotope dilution tandem mass spectrometry. Clin Chem. 2000 Oct;46(10):1650-6. [PubMed:11017945 ]
  6. Scalabrino G, Pigatto P, Ferioli ME, Modena D, Puerari M, Caru A: Levels of activity of the polyamine biosynthetic decarboxylases as indicators of degree of malignancy of human cutaneous epitheliomas. J Invest Dermatol. 1980 Mar;74(3):122-4. [PubMed:7359002 ]
  7. Kaneoka H, Uesugi N, Moriguchi A, Hirose S, Takayanagi M, Yamaguchi S, Shigematsu Y, Yasuno T, Sasatomi Y, Saito T: Carnitine palmitoyltransferase II deficiency due to a novel gene variant in a patient with rhabdomyolysis and ARF. Am J Kidney Dis. 2005 Mar;45(3):596-602. [PubMed:15754283 ]
  8. Rosen RT, Hiserodt RD, Fukuda EK, Ruiz RJ, Zhou Z, Lech J, Rosen SL, Hartman TG: The determination of metabolites of garlic preparations in breath and human plasma. Biofactors. 2000;13(1-4):241-9. [PubMed:11237188 ]
  9. McFadden PN, Horwitz J, Clarke S: Protein carboxyl methyltransferase from cow eye lens. Biochem Biophys Res Commun. 1983 Jun 15;113(2):418-24. [PubMed:6870865 ]
  10. Garibotto G, Sofia A, Valli A, Tarroni A, Di Martino M, Cappelli V, Aloisi F, Procopio V: Causes of hyperhomocysteinemia in patients with chronic kidney diseases. Semin Nephrol. 2006 Jan;26(1):3-7. [PubMed:16412817 ]
  11. Spiekerkoetter U, Tokunaga C, Wendel U, Mayatepek E, Ijlst L, Vaz FM, van Vlies N, Overmars H, Duran M, Wijburg FA, Wanders RJ, Strauss AW: Tissue carnitine homeostasis in very-long-chain acyl-CoA dehydrogenase-deficient mice. Pediatr Res. 2005 Jun;57(6):760-4. Epub 2005 Mar 17. [PubMed:15774826 ]
  12. Jones MG, Goodwin CS, Amjad S, Chalmers RA: Plasma and urinary carnitine and acylcarnitines in chronic fatigue syndrome. Clin Chim Acta. 2005 Oct;360(1-2):173-7. [PubMed:15967423 ]
  13. Kelm A, Shaw L, Schauer R, Reuter G: The biosynthesis of 8-O-methylated sialic acids in the starfish Asterias rubens--isolation and characterisation of S-adenosyl-L-methionine:sialate-8-O-methyltransferase. Eur J Biochem. 1998 Feb 1;251(3):874-84. [PubMed:9490063 ]
  14. Solano AR, Sanchez ML, Podesta EJ, Turyn D, Dellacha JM: Membrane methylation in isolated rat testis interstitial cells unmasks functional luteinizing hormone receptors. Biochim Biophys Acta. 1987 Apr 2;928(1):107-13. [PubMed:3828399 ]
  15. D'Erme M, Santoro R, Allegra P, Reale A, Marenzi S, Strom R, Caiafa P: Inhibition of CpG methylation in linker DNA by H1 histone. Biochim Biophys Acta. 1993 May 28;1173(2):209-16. [PubMed:8504169 ]
  16. Scott JM, Weir DG: The methyl folate trap. A physiological response in man to prevent methyl group deficiency in kwashiorkor (methionine deficiency) and an explanation for folic-acid induced exacerbation of subacute combined degeneration in pernicious anaemia. Lancet. 1981 Aug 15;2(8242):337-40. [PubMed:6115113 ]

Only showing the first 10 proteins. There are 129 proteins in total.


General function:
Involved in N-methyltransferase activity
Specific function:
Catalyzes three sequential methylation reactions of phosphatidylethanolamine (PE) by AdoMet, thereby producing phosphatidylcholine (PC).
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + phosphatidyl-N-methylethanolamine → S-Adenosylhomocysteine + phosphatidyl-N-dimethylethanolaminedetails
S-Adenosylmethionine + phosphatidyl-N-dimethylethanolamine → S-Adenosylhomocysteine + phosphatidylcholinedetails
S-Adenosylmethionine + Phosphatidylethanolamine → S-Adenosylhomocysteine + phosphatidyl-N-methylethanolaminedetails
S-Adenosylmethionine + Phosphatidyl-N-dimethylethanolamine → S-Adenosylhomocysteine + Phosphatidylcholinedetails
S-Adenosylmethionine + Phosphatidylethanolamine → S-Adenosylhomocysteine + Phosphatidyl-N-methylethanolaminedetails
General function:
Involved in O-methyltransferase activity
Specific function:
Isoform 1 catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine). Isoform 2 and isoform 3 lack enzyme activity.
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + N-Acetylserotonin → S-Adenosylhomocysteine + Melatonindetails
S-Adenosylmethionine + 5-Hydroxyindoleacetic acid → S-Adenosylhomocysteine + 5-Methoxyindoleacetatedetails
General function:
Involved in cobalamin binding
Specific function:
Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity).
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in magnesium ion binding
Specific function:
Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + a catechol → S-Adenosylhomocysteine + a guaiacoldetails
S-Adenosylmethionine + Norepinephrine → S-Adenosylhomocysteine + Normetanephrinedetails
S-Adenosylmethionine + Epinephrine → S-Adenosylhomocysteine + Metanephrinedetails
S-Adenosylmethionine + 3,4-Dihydroxybenzeneacetic acid → S-Adenosylhomocysteine + Homovanillic aciddetails
S-Adenosylmethionine + Dopamine → S-Adenosylhomocysteine + 3-Methoxytyraminedetails
2-Hydroxyestrone + S-Adenosylmethionine → 2-Methoxyestrone + S-Adenosylhomocysteinedetails
2-Hydroxyestradiol + S-Adenosylmethionine → 2-Methoxyestradiol + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + 3,4-Dihydroxyphenylglycol → S-Adenosylhomocysteine + Vanylglycoldetails
S-Adenosylmethionine + 3,4-Dihydroxymandelic acid → S-Adenosylhomocysteine + Vanillylmandelic aciddetails
General function:
Involved in DNA binding
Specific function:
Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA.
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + L-lysine-[histone] → S-Adenosylhomocysteine + N(6)-methyl-L-lysine-[histone]details
Protein lysine + S-Adenosylmethionine → Protein N6-methyl-L-lysine + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + Protein N6-methyl-L-lysine → S-Adenosylhomocysteine + Protein N6,N6-dimethyl-L-lysinedetails
S-Adenosylmethionine + Protein N6,N6-dimethyl-L-lysine → S-Adenosylhomocysteine + Protein N6,N6,N6-trimethyl-L-lysinedetails
General function:
Involved in folic acid binding
Specific function:
Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine.
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + Glycine → S-Adenosylhomocysteine + Sarcosinedetails
General function:
Involved in histone-lysine N-methyltransferase activity
Specific function:
Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + L-lysine-[histone] → S-Adenosylhomocysteine + N(6)-methyl-L-lysine-[histone]details
Protein lysine + S-Adenosylmethionine → Protein N6-methyl-L-lysine + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + Protein N6-methyl-L-lysine → S-Adenosylhomocysteine + Protein N6,N6-dimethyl-L-lysinedetails
S-Adenosylmethionine + Protein N6,N6-dimethyl-L-lysine → S-Adenosylhomocysteine + Protein N6,N6,N6-trimethyl-L-lysinedetails
General function:
Involved in methionine adenosyltransferase activity
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Gene Name:
Uniprot ID:
Molecular weight:
Adenosine triphosphate + L-Methionine + Water → Phosphoric acid + Pyrophosphate + S-Adenosylmethioninedetails
Phosphoric acid + Pyrophosphate + S-Adenosylmethionine → Adenosine triphosphate + L-Methionine + Waterdetails
General function:
Involved in methyltransferase activity
Specific function:
Converts noradrenaline to adrenaline.
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + 2-Hydroxyphenethylamine → S-Adenosylhomocysteine + N-Methylphenylethanolaminedetails
S-Adenosylmethionine + Norepinephrine → S-Adenosylhomocysteine + Epinephrinedetails
General function:
Involved in methyltransferase activity
Specific function:
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis (By similarity).
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + 2-(3-Carboxy-3-aminopropyl)-L-histidine → S-Adenosylhomocysteine + 2-(3-carboxy-3-(trimethylammonio)propyl)-L-histidinedetails

Only showing the first 10 proteins. There are 129 proteins in total.