You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Record Information
Version4.0
StatusDetected and Quantified
Creation Date2005-11-16 15:48:42 UTC
Update Date2018-05-20 20:24:34 UTC
HMDB IDHMDB0000939
Secondary Accession Numbers
  • HMDB00939
Metabolite Identification
Common NameS-Adenosylhomocysteine
DescriptionS-Adenosyl-L-homocysteine (SAH) is formed by the demethylation of S-adenosyl-L-methionine. S-Adenosylhomocysteine (AdoHcy or SAH) is also the immediate precursor of all of the homocysteine produced in the body. The reaction is catalyzed by S-adenosylhomocysteine hydrolase and is reversible with the equilibrium favoring formation of SAH. In vivo, the reaction is driven in the direction of homocysteine formation by the action of the enzyme adenosine deaminase which converts the second product of the S-adenosylhomocysteine hydrolase reaction, adenosine, to inosine. Except for methyl transfer from betaine and from methylcobalamin in the methionine synthase reaction, SAH is the product of all methylation reactions that involve S-adenosylmethionine (SAM) as the methyl donor. Methylation is significant in epigenetic regulation of protein expression via DNA and histone methylation. The inhibition of these SAM-mediated processes by SAH is a proven mechanism for metabolic alteration. Because the conversion of SAH to homocysteine is reversible, with the equilibrium favoring the formation of SAH, increases in plasma homocysteine are accompanied by an elevation of SAH in most cases. Disturbances in the transmethylation pathway indicated by abnormal SAH, SAM, or their ratio have been reported in many neurodegenerative diseases, such as dementia, depression, and Parkinson's disease (PMID: 18065573 , 17892439 ). Therefore, when present in sufficiently high levels, S-adenosylhomocysteine can act as an immunotoxin and a metabotoxin. An immunotoxin disrupts, limits the function, or destroys immune cells. A metabotoxin is an endogenous metabolite that causes adverse health effects at chronically high levels. Chronically high levels of S-adenosylhomocysteine are associated with S-adenosylhomocysteine (SAH) hydrolase deficiency and adenosine deaminase deficiency. S-Adenosylhomocysteine forms when there are elevated levels of homocysteine and adenosine. S-Adenosyl-L-homocysteine is a potent inhibitor of S-adenosyl-L-methionine-dependent methylation reactions. It is toxic to immature lymphocytes and can lead to immunosuppression (PMID: 221926 ).
Structure
Thumb
Synonyms
ValueSource
(2S)-2-amino-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}sulfanyl)butanoic acidChEBI
2-S-Adenosyl-L-homocysteineChEBI
Adenosyl-L-homocysteineChEBI
AdenosylhomocysteineChEBI
AdoHcyChEBI
S-(5'-Adenosyl)-L-homocysteineChEBI
S-[1-(Adenin-9-yl)-1,5-dideoxy-beta-D-ribofuranos-5-yl]-L-homocysteineChEBI
SAHChEBI
(2S)-2-amino-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}sulfanyl)butanoateGenerator
(2S)-2-amino-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}sulphanyl)butanoateGenerator
(2S)-2-amino-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}sulphanyl)butanoic acidGenerator
S-[1-(Adenin-9-yl)-1,5-dideoxy-b-D-ribofuranos-5-yl]-L-homocysteineGenerator
S-[1-(Adenin-9-yl)-1,5-dideoxy-β-D-ribofuranos-5-yl]-L-homocysteineGenerator
(S)-5'-(S)-(3-amino-3-Carboxypropyl)-5'-thioadenosineHMDB
5'-Deoxy-S-adenosyl-L-homocysteineHMDB
5'-S-(3-amino-3-Carboxypropyl)-5'-thio-L-adenosineHMDB
Adenosyl-homo-cysHMDB
adenosylhomo-CYSHMDB
FormycinylhomocysteineHMDB
L-5'-S-(3-amino-3-Carboxypropyl)-5'-thior-adenosineHMDB
L-S-Adenosyl-homocysteineHMDB
L-S-AdenosylhomocysteineHMDB
S-(5'-Deoxyadenosin-5'-yl)-L-homocysteineHMDB
S-(5'-Deoxyadenosine-5')-L-homocysteineHMDB
S-Adenosyl-homocysteineHMDB
S-Adenosyl-L-homocysteineHMDB
Adenosylhomocysteine, SMeSH
S AdenosylhomocysteineMeSH
Chemical FormulaC14H20N6O5S
Average Molecular Weight384.411
Monoisotopic Molecular Weight384.12158847
IUPAC Name(2S)-2-amino-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl}sulfanyl)butanoic acid
Traditional NameS-adenosyl-L-homocysteine
CAS Registry Number979-92-0
SMILES
N[C@@H](CCSC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC2=C1N=CN=C2N)C(O)=O
InChI Identifier
InChI=1S/C14H20N6O5S/c15-6(14(23)24)1-2-26-3-7-9(21)10(22)13(25-7)20-5-19-8-11(16)17-4-18-12(8)20/h4-7,9-10,13,21-22H,1-3,15H2,(H,23,24)(H2,16,17,18)/t6-,7+,9+,10+,13+/m0/s1
InChI KeyZJUKTBDSGOFHSH-WFMPWKQPSA-N
Chemical Taxonomy
DescriptionThis compound belongs to the class of organic compounds 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.
KingdomOrganic compounds
Super ClassNucleosides, nucleotides, and analogues
Class5'-deoxyribonucleosides
Sub Class5'-deoxy-5'-thionucleosides
Direct Parent5'-deoxy-5'-thionucleosides
Alternative Parents
Substituents
  • 5'-deoxy-5'-thionucleoside
  • 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
  • Pyrimidine
  • Fatty acyl
  • Monosaccharide
  • Imidolactam
  • N-substituted imidazole
  • Tetrahydrofuran
  • Imidazole
  • Azole
  • Heteroaromatic compound
  • Secondary alcohol
  • Amino acid or derivatives
  • Amino acid
  • 1,2-diol
  • Oxacycle
  • Azacycle
  • Carboxylic acid derivative
  • Carboxylic acid
  • Organoheterocyclic compound
  • Dialkylthioether
  • Sulfenyl compound
  • Thioether
  • Monocarboxylic acid or derivatives
  • Organic oxide
  • Organopnictogen compound
  • Alcohol
  • Carbonyl group
  • Organic oxygen compound
  • Amine
  • Hydrocarbon derivative
  • Organic nitrogen compound
  • Primary amine
  • Primary aliphatic amine
  • Organosulfur compound
  • Organooxygen compound
  • Organonitrogen compound
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Ontology
Physiological effect

Health effect:

Disposition

Route of exposure:

Source:

Biological location:

Process

Naturally occurring process:

Role

Indirect biological role:

Industrial application:

Biological role:

Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point209 - 211 °CNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
Water Solubility4.08 g/LALOGPS
logP-2.4ALOGPS
logP-4ChemAxon
logS-2ALOGPS
pKa (Strongest Acidic)1.81ChemAxon
pKa (Strongest Basic)9.5ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count10ChemAxon
Hydrogen Donor Count5ChemAxon
Polar Surface Area182.63 ŲChemAxon
Rotatable Bond Count7ChemAxon
Refractivity92.72 m³·mol⁻¹ChemAxon
Polarizability38.41 ųChemAxon
Number of Rings3ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash Key
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0a6u-9853000000-441f171739659ea2b5f6View in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (3 TMS) - 70eV, Positivesplash10-004r-7096060000-d32383fe3b85ef1b9032View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0006-0943000000-80fa5c7d919e1085bc5dView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-00di-0900000000-3f143852503952daa0a8View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-03di-0900000000-23694a4b657a3478ad91View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0udr-0980000000-a8f61dcdc8693e2725f5View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-00kf-0974000000-b3f3632635b2847bf4d2View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-00di-0900000000-188a77c79aaefae8a184View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-000i-0900000000-b848c20d743785117445View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0udr-0980000000-64b7b303fc07300e0782View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-001i-0319020200-859d659a39a790a582f1View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a4i-0900000000-53acf4e10681047da062View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-001i-0910000000-5896502e31d66786e12aView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-001i-0009000000-01ea51599f8d30dec7feView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-001i-0409000100-2de58945ab0dfa81f099View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a4i-1900000000-a640f1a0bafd33afdd2dView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-001i-0910000000-5f685035af9b243ccff2View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-001i-0009000000-8d01fd0969e47d3bcc5cView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , Positivesplash10-000i-2901000000-6c40a4a43a8c3e142eceView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , Negativesplash10-001i-0902000000-c6c0d5529cf011d89f7bView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT , negativesplash10-0a4i-0900000000-53acf4e10681047da062View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000i-1905000000-71a19cb77ac6797e6d81View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-1900000000-11e0ecd68eec9b6ef4f5View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-5900000000-c10849015d4b1c3ef749View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-001i-0925000000-384762ca7868d8aa06ddView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-001i-1900000000-2fb047bdcd6fb31842eaView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-053r-2900000000-a6bc4489e6fe48ead399View in MoNA
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
2D NMR[1H,1H] 2D NMR SpectrumNot AvailableView in JSpectraViewer
2D NMR[1H,13C] 2D NMR SpectrumNot AvailableView in JSpectraViewer
Biological Properties
Cellular Locations
  • Mitochondria
  • Nucleus
  • Endoplasmic reticulum
Biospecimen Locations
  • Blood
  • Cerebrospinal Fluid (CSF)
  • Feces
  • Urine
Tissue Location
  • Kidney
  • Liver
  • Lymphoblast
  • Myelin
  • Neuron
  • Placenta
  • Prostate
Pathways
Normal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified0.46 +/- 0.02 uMElderly (>65 years old)BothNormal details
BloodDetected and Quantified0.00900-0.0450 uMNot SpecifiedNot Specified
Normal
details
Cerebrospinal Fluid (CSF)Detected and Quantified0.00100-0.0290 uMNot SpecifiedNot Specified
Normal
details
Cerebrospinal Fluid (CSF)Detected and Quantified0.01 (0.009-0.014) uMAdult (>18 years old)BothNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified0.0243 +/- 0.0068 uMNot SpecifiedNot SpecifiedNormal details
UrineExpected but not Quantified Not AvailableNot AvailableNormal
    details
    Abnormal Concentrations
    BiospecimenStatusValueAgeSexConditionReferenceDetails
    BloodDetected and Quantified0.016 (0.009-0.025) uMAdult (>18 years old)BothNeurodegenerative diseases details
    BloodDetected and Quantified0.49 +/- 0.05 uMElderly (>65 years old)BothParkinson's Disease details
    BloodDetected and Quantified0.102 uMAdolescent (13-18 years old)Female
    Adenosine kinase deficiency
    details
    BloodDetected and Quantified0.122 uMAdult (>18 years old)Male
    Adenosine kinase deficiency
    details
    Cerebrospinal Fluid (CSF)Detected and Quantified0.0269 +/- 0.0062 uMAdult (>18 years old)Not SpecifiedAlzheimer's disease details
    Cerebrospinal Fluid (CSF)Detected and Quantified0.068 uMAdolescent (13-18 years old)Female
    Adenosine kinase deficiency
    details
    Cerebrospinal Fluid (CSF)Detected and Quantified0.102 uMAdult (>18 years old)Male
    Adenosine kinase deficiency
    details
    FecesDetected but not Quantified Children (6 - 18 years old)Bothenthesitis-related arthritis details
    UrineDetected and Quantified0.882 +/- 0.075 umol/mmol creatinineChildren (1 - 13 years old)Not Specified
    Eosinophilic esophagitis
      • Mordechai, Hien, ...
    details
    Associated Disorders and Diseases
    Disease References
    Alzheimer's disease
    1. Linnebank M, Popp J, Smulders Y, Smith D, Semmler A, Farkas M, Kulic L, Cvetanovska G, Blom H, Stoffel-Wagner B, Kolsch H, Weller M, Jessen F: S-adenosylmethionine is decreased in the cerebrospinal fluid of patients with Alzheimer's disease. Neurodegener Dis. 2010;7(6):373-8. doi: 10.1159/000309657. Epub 2010 Jun 3. [PubMed:20523031 ]
    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 ]
    Parkinson's disease
    1. Cheng H, Gomes-Trolin C, Aquilonius SM, Steinberg A, Lofberg C, Ekblom J, Oreland L: Levels of L-methionine S-adenosyltransferase activity in erythrocytes and concentrations of S-adenosylmethionine and S-adenosylhomocysteine in whole blood of patients with Parkinson's disease. Exp Neurol. 1997 Jun;145(2 Pt 1):580-5. [PubMed:9217094 ]
    Eosinophilic esophagitis
    1. (). Mordechai, Hien, and David S. Wishart. .
    Adenosine kinase deficiency
    1. Bjursell MK, Blom HJ, Cayuela JA, Engvall ML, Lesko N, Balasubramaniam S, Brandberg G, Halldin M, Falkenberg M, Jakobs C, Smith D, Struys E, von Dobeln U, Gustafsson CM, Lundeberg J, Wedell A: Adenosine kinase deficiency disrupts the methionine cycle and causes hypermethioninemia, encephalopathy, and abnormal liver function. Am J Hum Genet. 2011 Oct 7;89(4):507-15. doi: 10.1016/j.ajhg.2011.09.004. Epub 2011 Sep 28. [PubMed:21963049 ]
    Associated OMIM IDs
    DrugBank IDNot Available
    Phenol Explorer Compound IDNot Available
    FoodDB IDFDB022327
    KNApSAcK IDC00007230
    Chemspider ID388301
    KEGG Compound IDC00021
    BioCyc IDADENOSYL-HOMO-CYS
    BiGG ID33543
    Wikipedia LinkS-Adenosyl-L-homocysteine
    METLIN ID296
    PubChem Compound439155
    PDB IDSAH
    ChEBI ID16680
    References
    Synthesis ReferenceHoly, Antonin; Rosenberg, Ivan. Studies on S-adenosyl-L-homocysteine hydrolase. Part XV. An improved synthesis of S-adenosyl-L-homocysteine and related compounds. Collection of Czechoslovak Chemical Communications (1985), 50(7), 1514-18.
    Material Safety Data Sheet (MSDS)Download (PDF)
    General References
    1. Augoustides-Savvopoulou P, Luka Z, Karyda S, Stabler SP, Allen RH, Patsiaoura K, Wagner C, Mudd SH: Glycine N -methyltransferase deficiency: a new patient with a novel mutation. J Inherit Metab Dis. 2003;26(8):745-59. [PubMed:14739680 ]
    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. Hershfield MS, Kredich NM, Koller CA, Mitchell BS, Kurtzberg J, Kinney TR, Falletta JM: S-adenosylhomocysteine catabolism and basis for acquired resistance during treatment of T-cell acute lymphoblastic leukemia with 2'-deoxycoformycin alone and in combination with 9-beta-D-arabinofuranosyladenine. Cancer Res. 1983 Jul;43(7):3451-8. [PubMed:6601986 ]
    4. Miller AL: The methionine-homocysteine cycle and its effects on cognitive diseases. Altern Med Rev. 2003 Feb;8(1):7-19. [PubMed:12611557 ]
    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. Wang J, Dudman NP, Wilcken DE: Effects of homocysteine and related compounds on prostacyclin production by cultured human vascular endothelial cells. Thromb Haemost. 1993 Dec 20;70(6):1047-52. [PubMed:8165599 ]
    7. Palella TD, Schatz RA, Wilens TE, Fox IH: S-Adenosylhomocysteine accumulation and selective cytotoxicity in cultured T- and B-lymphocytes. J Lab Clin Med. 1982 Aug;100(2):269-78. [PubMed:6980250 ]
    8. van Guldener C, Stehouwer CD: Homocysteine and methionine metabolism in renal failure. Semin Vasc Med. 2005 May;5(2):201-8. [PubMed:16047272 ]
    9. Muskiet FA: The importance of (early) folate status to primary and secondary coronary artery disease prevention. Reprod Toxicol. 2005 Sep-Oct;20(3):403-10. [PubMed:15964170 ]
    10. Fowler B: Homocysteine: overview of biochemistry, molecular biology, and role in disease processes. Semin Vasc Med. 2005 May;5(2):77-86. [PubMed:16047261 ]
    11. Gordon RK, Ginalski K, Rudnicki WR, Rychlewski L, Pankaskie MC, Bujnicki JM, Chiang PK: Anti-HIV-1 activity of 3-deaza-adenosine analogs. Inhibition of S-adenosylhomocysteine hydrolase and nucleotide congeners. Eur J Biochem. 2003 Sep;270(17):3507-17. [PubMed:12919315 ]
    12. Metz J: Cobalamin deficiency and the pathogenesis of nervous system disease. Annu Rev Nutr. 1992;12:59-79. [PubMed:1354465 ]
    13. Mulder C, Schoonenboom NS, Jansen EE, Verhoeven NM, van Kamp GJ, Jakobs C, Scheltens P: The transmethylation cycle in the brain of Alzheimer patients. Neurosci Lett. 2005 Sep 30;386(2):69-71. [PubMed:16040194 ]
    14. Delabar U, Kloor D, Luippold G, Muhlbauer B: Simultaneous determination of adenosine, S-adenosylhomocysteine and S-adenosylmethionine in biological samples using solid-phase extraction and high-performance liquid chromatography. J Chromatogr B Biomed Sci Appl. 1999 Mar 19;724(2):231-8. [PubMed:10219663 ]
    15. Hermes M, von Hippel S, Osswald H, Kloor D: S-adenosylhomocysteine metabolism in different cell lines: effect of hypoxia and cell density. Cell Physiol Biochem. 2005;15(5):233-44. [PubMed:15956786 ]
    16. Weir DG, Molloy AM, Keating JN, Young PB, Kennedy S, Kennedy DG, Scott JM: Correlation of the ratio of S-adenosyl-L-methionine to S-adenosyl-L-homocysteine in the brain and cerebrospinal fluid of the pig: implications for the determination of this methylation ratio in human brain. Clin Sci (Lond). 1992 Jan;82(1):93-7. [PubMed:1310924 ]
    17. Wagner C, Koury MJ: S-Adenosylhomocysteine: a better indicator of vascular disease than homocysteine? Am J Clin Nutr. 2007 Dec;86(6):1581-5. [PubMed:18065573 ]
    18. Herrmann W, Obeid R: Biomarkers of folate and vitamin B(12) status in cerebrospinal fluid. Clin Chem Lab Med. 2007;45(12):1614-20. [PubMed:17892439 ]
    19. Kredich NM, Hershfield MS: S-adenosylhomocysteine toxicity in normal and adenosine kinase-deficient lymphoblasts of human origin. Proc Natl Acad Sci U S A. 1979 May;76(5):2450-4. [PubMed:221926 ]

    Only showing the first 10 proteins. There are 94 proteins in total.

    Enzymes

    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:
    PEMT
    Uniprot ID:
    Q9UBM1
    Molecular weight:
    23697.395
    Reactions
    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:
    ASMT
    Uniprot ID:
    P46597
    Molecular weight:
    41660.34
    Reactions
    S-Adenosylmethionine + N-Acetylserotonin → S-Adenosylhomocysteine + Melatonindetails
    S-Adenosylmethionine + 5-Hydroxyindoleacetic acid → S-Adenosylhomocysteine + 5-Methoxyindoleacetatedetails
    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:
    COMT
    Uniprot ID:
    P21964
    Molecular weight:
    30036.77
    Reactions
    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:
    DOT1L
    Uniprot ID:
    Q8TEK3
    Molecular weight:
    164854.41
    Reactions
    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:
    GNMT
    Uniprot ID:
    Q14749
    Molecular weight:
    32742.0
    Reactions
    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:
    SETD7
    Uniprot ID:
    Q8WTS6
    Molecular weight:
    40720.595
    Reactions
    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 methyltransferase activity
    Specific function:
    Converts noradrenaline to adrenaline.
    Gene Name:
    PNMT
    Uniprot ID:
    P11086
    Molecular weight:
    30854.745
    Reactions
    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:
    DPH5
    Uniprot ID:
    Q9H2P9
    Molecular weight:
    31651.17
    Reactions
    S-Adenosylmethionine + 2-(3-Carboxy-3-aminopropyl)-L-histidine → S-Adenosylhomocysteine + 2-(3-carboxy-3-(trimethylammonio)propyl)-L-histidinedetails
    General function:
    Involved in methyltransferase activity
    Specific function:
    Catalyzes the transfer of a methyl group from AdoMet to trivalent arsenicals producing methylated and dimethylated arsenicals. It methylates arsenite to form methylarsonate, Me-AsO(3)H(2), which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite is also a substrate and it is converted into the much less toxic compound dimethylarsinate (cacodylate), Me(2)As(O)-OH (By similarity).
    Gene Name:
    AS3MT
    Uniprot ID:
    Q9HBK9
    Molecular weight:
    41747.49
    Reactions
    S-Adenosylmethionine + Arsenite → S-Adenosylhomocysteine + Methylarsonatedetails
    S-Adenosylmethionine + Methylarsonite → S-Adenosylhomocysteine + Dimethylarsinatedetails
    General function:
    Involved in transferase activity
    Specific function:
    Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2- thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base
    Gene Name:
    TRMU
    Uniprot ID:
    O75648
    Molecular weight:
    47744.3

    Only showing the first 10 proteins. There are 94 proteins in total.