Record Information
Version2.0
Creation Date2012-05-31 13:47:10 -0600
Update Date2015-10-15 16:13:52 -0600
Secondary Accession Numbers
  • ECMDB01185
Identification
Name:S-Adenosylmethionine
Description:S-Adenosylmethionine is a physiologic methyl radical donor involved in enzymatic transmethylation reactions and present in all living organisms. It is made from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase (EC 2.5.1.6). Transmethylation, transsulfuration, and aminopropylation are the metabolic pathways that use S-Adenosylmethionine. In bacteria, SAM is bound by the SAM riboswitch, which regulates genes involved in methionine or cysteine biosynthesis. (Wikipedia)
Structure
Thumb
Synonyms:
  • (3S)-5'-[(3-amino-3-carboxypropyl)methylsulfonio]-5'-deoxyadenosine
  • (3S)-5'-[(3-amino-3-carboxypropyl)methylsulphonio]-5'-deoxyadenosine
  • 2-S-adenosyl-L-methionine
  • 2-S-Adenosyl-L-methionine
  • 5'-Deoxyadenosine-5'-L-methionine disulfate ditosylate
  • 5'-Deoxyadenosine-5'-L-methionine disulfuric acid ditosylic acid
  • 5'-Deoxyadenosine-5'-L-methionine disulphate ditosylate
  • 5'-Deoxyadenosine-5'-L-methionine disulphuric acid ditosylic acid
  • S-adenosyl-methionine
  • S-adenosylmethionine
  • Active methionine
  • Ademetionine
  • Adenosylmethionine
  • AdoMet
  • Donamet
  • L-S-Adenosylmethionine
  • S-(5'-Adenosyl)-L-methionine
  • S-(5'-Deoxyadenosin-5'-yl)-L-methionine
  • S-Adenosyl methionine
  • S-Adenosyl-L-methionine
  • S-Adenosyl-L-Methionine Disulfate Tosylate
  • S-Adenosyl-L-methionine disulfuric acid tosylic acid
  • S-Adenosyl-L-methionine disulphate tosylate
  • S-Adenosyl-L-methionine disulphuric acid tosylic acid
  • S-Adenosyl-methionine
  • S-Adenosylmethionine
  • SAM
Chemical Formula:C15H23N6O5S
Weight:Average: 399.445
Monoisotopic: 399.145063566
InChI Key:MEFKEPWMEQBLKI-AIRLBKTGSA-O
InChI:InChI=1S/C15H22N6O5S/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25)/p+1/t7-,8+,10+,11+,14+,27?/m0/s1
CAS number:29908-03-0
IUPAC Name:[(3R)-3-amino-3-carboxypropyl]({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl})methylsulfanium
Traditional IUPAC Name:[(3R)-3-amino-3-carboxypropyl]({[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl})methylsulfanium
SMILES:C[S+](CC[C@H](N)C(O)=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC2=C(N)N=CN=C12
Chemical Taxonomy
DescriptionThis compound belongs to the class of organic compounds known as glycosylamines. These are compounds consisting of an amine with a beta-N-glycosidic bond to a carbohydrate, thus forming a cyclic hemiaminal ether bond (alpha-amino ether).
KingdomOrganic compounds
Super ClassOrganooxygen compounds
ClassCarbohydrates and carbohydrate conjugates
Sub ClassGlycosyl compounds
Direct ParentGlycosylamines
Alternative Parents
Substituents
  • N-glycosyl compound
  • D-alpha-amino acid
  • Methionine or derivatives
  • Alpha-amino acid or derivatives
  • Alpha-amino acid
  • 6-aminopurine
  • Purine
  • Imidazopyrimidine
  • Thia fatty acid
  • Aminopyrimidine
  • Amino fatty acid
  • Fatty acyl
  • Imidolactam
  • Pyrimidine
  • Primary aromatic amine
  • N-substituted imidazole
  • Monosaccharide
  • Heteroaromatic compound
  • Oxolane
  • Imidazole
  • Azole
  • Secondary alcohol
  • 1,2-diol
  • Oxacycle
  • Azacycle
  • Organoheterocyclic compound
  • Monocarboxylic acid or derivatives
  • Carboxylic acid
  • Carboxylic acid derivative
  • Hydrocarbon derivative
  • Primary amine
  • Organosulfur compound
  • Organonitrogen compound
  • Primary aliphatic amine
  • Carbonyl group
  • Amine
  • Alcohol
  • Organic cation
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External DescriptorsNot Available
Physical Properties
State:Solid
Charge:1
Melting point:Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility1.19 mg/mLALOGPS
logP-2ALOGPS
logP-5.3ChemAxon
logS-2.6ALOGPS
pKa (Strongest Acidic)1.71ChemAxon
pKa (Strongest Basic)9.41ChemAxon
Physiological Charge1ChemAxon
Hydrogen Acceptor Count10ChemAxon
Hydrogen Donor Count5ChemAxon
Polar Surface Area182.63 Å2ChemAxon
Rotatable Bond Count7ChemAxon
Refractivity96.23 m3·mol-1ChemAxon
Polarizability39.84 Å3ChemAxon
Number of Rings3ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
2 S-Adenosylmethionine + Uroporphyrinogen III >2 S-Adenosylhomocysteine + Precorrin 2 + Hydrogen ion
S-Adenosylmethionine + Hydrogen ion <> S-Adenosylmethioninamine + Carbon dioxide
S-Adenosylmethionine + L-Homocysteine + S-Methylmethionine <> S-Adenosylhomocysteine + Hydrogen ion + L-Methionine
[4Fe-4S] iron-sulfur cluster + 2 S-Adenosylmethionine + Hydrogen ion + NAD + octanoate (protein bound) > [2Fe-2S] iron-sulfur cluster +2 5'-Deoxyadenosine +2 Iron + lipoate (protein bound) +2 L-Methionine + NADH
8-Amino-7-oxononanoate + S-Adenosylmethionine <> S-Adenosyl-4-methylthio-2-oxobutanoate + 7,8-Diaminononanoate
[2Fe-2S] iron-sulfur cluster + S-Adenosylmethionine + Dethiobiotin > [2Fe-1S] desulfurated iron-sulfur cluster + Biotin + 5'-Deoxyadenosine + Hydrogen ion + L-Methionine
S-Adenosylmethionine + Malonyl-CoA > S-Adenosylhomocysteine + malonyl-CoA methyl ester
trans-Aconitic acid + S-Adenosylmethionine > E-3-Carboxy-2-pentenedioate 6-methyl ester + S-Adenosylhomocysteine
2 S-Adenosylmethionine + PE(14:0/14:0) >2 S-Adenosylhomocysteine + Cyclopropane phosphatidylethanolamine (dihexadec-9,10-cyclo-anoyl, N-C16:0 cyclo) +2 Hydrogen ion
2 S-Adenosylmethionine + PE(14:0/14:0) >2 S-Adenosylhomocysteine + Cyclopropane phosphatidylethanolamine (dioctadec-11,12-cyclo-anoyl, N-C18:0 cyclo) +2 Hydrogen ion
2 S-Adenosylmethionine + PG(16:1(9Z)/16:1(9Z)) >2 S-Adenosylhomocysteine + Cyclopropane phosphatidylglycerol (dihexadec-9,10-cyclo-anoyl, N-C16:0 cyclo) +2 Hydrogen ion
2 S-Adenosylmethionine + PG(18:1(11Z)/18:1(11Z)) >2 S-Adenosylhomocysteine + Cyclopropane phosphatidylglycerol (dioctadec-11,12-cyclo-anoyl, N-C18:0 cyclo) +2 Hydrogen ion
2-Octaprenyl-6-hydroxyphenol + S-Adenosylmethionine > 2-Octaprenyl-6-methoxyphenol + S-Adenosylhomocysteine + Hydrogen ion
2-Octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinol + S-Adenosylmethionine > S-Adenosylhomocysteine + Hydrogen ion + Ubiquinol-8
Adenosine triphosphate + Water + L-Methionine <> S-Adenosylmethionine + Phosphate + Pyrophosphate
2-Demethylmenaquinol 8 + S-Adenosylmethionine > S-Adenosylhomocysteine + Hydrogen ion + Menaquinol 8
2-Octaprenyl-6-methoxy-1,4-benzoquinol + S-Adenosylmethionine > 2-Octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol + S-Adenosylhomocysteine + Hydrogen ion
2 S-Adenosylmethionine + Coproporphyrin III <>2 Carbon dioxide +2 5'-Deoxyadenosine +2 L-Methionine + Protoporphyrinogen IX
S-Adenosylmethionine + NADPH + L-Tyrosine > p-Cresol + 5'-Deoxyadenosine + Dehydroglycine + Hydrogen ion + L-Methionine + NADP
Phosphate + Pyrophosphate + S-Adenosylmethionine <> Adenosine triphosphate + L-Methionine + Water
S-Adenosylmethionine + Hydrogen ion <> S-Adenosylmethioninamine + Carbon dioxide
S-Adenosylmethionine + L-Homocysteine <> S-Adenosylhomocysteine + L-Methionine
Dethiobiotin + Sulfur donor + 2 S-Adenosylmethionine + 2 e- + 2 Hydrogen ion <> Biotin +2 L-Methionine +2 5'-Deoxyadenosine
2 S-Adenosylmethionine + Uroporphyrinogen III <>2 S-Adenosylhomocysteine + Precorrin 2
S-Adenosylmethionine + 8-Amino-7-oxononanoate <> S-Adenosyl-4-methylthio-2-oxobutanoate + 7,8-Diaminononanoate
4-Amino-5-hydroxymethyl-2-methylpyrimidine + S-Adenosylmethionine <> 5-Aminoimidazole ribonucleotide + 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + CO
S-Adenosylmethionine + DNA cytosine <> S-Adenosylhomocysteine + DNA 5-methylcytosine
2-Octaprenyl-6-hydroxyphenol + S-Adenosylmethionine <> 2-Octaprenyl-6-methoxyphenol + S-Adenosylhomocysteine
2-octaprenyl-6-methoxy-1,4-benzoquinone + S-Adenosylmethionine <> 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-Adenosylhomocysteine
2-Demethylmenaquinone 8 + S-Adenosylmethionine <> Menaquinone + S-Adenosylhomocysteine
2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone + S-Adenosylmethionine <> Ubiquinone-8 + S-Adenosylhomocysteine
2-Phytyl-1,4-naphthoquinone + S-Adenosylmethionine <> Phylloquinone + S-Adenosylhomocysteine
Coproporphyrin III + 2 S-Adenosylmethionine <> Protoporphyrinogen IX +2 Carbon dioxide +2 L-Methionine +2 5'-Deoxyadenosine
S-Adenosylmethionine + rRNA <> S-Adenosylhomocysteine + rRNA containing N6-methyladenine
S-Adenosylmethionine + rRNA <> S-Adenosylhomocysteine + rRNA containing N1-methylguanine
S-Adenosylmethionine + rRNA <> S-Adenosylhomocysteine + rRNA containing N2-methylguanine
Protein N6-(octanoyl)lysine + 2 Sulfur donor + 2 S-Adenosylmethionine + Protein N6-(octanoyl)lysine <> Protein N6-(lipoyl)lysine +2 L-Methionine +2 5'-Deoxyadenosine + Protein N6-(lipoyl)lysine
Octanoyl-[acp] + 2 Sulfur donor + 2 S-Adenosylmethionine <> Lipoyl-[acp] +2 L-Methionine +2 5'-Deoxyadenosine
2-Polyprenyl-6-hydroxyphenol + S-Adenosylmethionine <> 2-Polyprenyl-6-methoxyphenol + S-Adenosylhomocysteine
2-Polyprenyl-6-methoxy-1,4-benzoquinone + S-Adenosylmethionine <> 2-Polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-Adenosylhomocysteine
2-Polyprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone + S-Adenosylmethionine <> Ubiquinone-1 + S-Adenosylhomocysteine
Demethylmenaquinol + S-Adenosylmethionine + Demethylmenaquinol <> Menaquinol 6 + S-Adenosylhomocysteine
S-Adenosylmethionine + precorrin-1 > S-Adenosylhomocysteine + Precorrin 2
S-Adenosylmethionine + a [protein]-L-glutamine > Hydrogen ion + S-Adenosylhomocysteine + a [protein]-N<sup>5</sup>-methyl-L-glutamine
tellurite + S-Adenosylmethionine methylated tellurite + S-Adenosylhomocysteine
Hydrogen ion + &alpha;-D-ribose-1-methylphosphonate-5-phosphate + S-Adenosylmethionine > &alpha;-D-ribose-1,2-cyclic-phosphate-5-phosphate + methane + 5'-Deoxyadenosine + L-Methionine
S-Adenosylmethionine + Uroporphyrinogen III <> S-Adenosylhomocysteine + precorrin-1 + Hydrogen ion
2-Octaprenyl-6-hydroxyphenol + S-Adenosylmethionine > Hydrogen ion + 2-Octaprenyl-6-methoxyphenol + S-Adenosylhomocysteine
2-Octaprenyl-6-methoxy-1,4-benzoquinol + S-Adenosylmethionine > Hydrogen ion + 2-Octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol + S-Adenosylhomocysteine
S-Adenosylmethionine + a [protein]-L-&beta;-isoaspartate > S-Adenosylhomocysteine + a protein L-&beta;-isoaspartate &alpha;-methyl ester + Hydrogen ion
a phospholipid olefinic fatty acid + S-Adenosylmethionine > a phospholipid cyclopropane fatty acid + S-Adenosylhomocysteine + Hydrogen ion
<i>S</i>-sulfanyl-[acceptor] + Dethiobiotin + S-Adenosylmethionine > an unsulfurated sulfur acceptor + Biotin + 5'-Deoxyadenosine + L-Methionine + Hydrogen ion
2-Demethylmenaquinol 8 + S-Adenosylmethionine > Menaquinol 8 + Hydrogen ion + S-Adenosylhomocysteine
S-Adenosylmethionine + 8-Amino-7-oxononanoate > S-Adenosyl-4-methylthio-2-oxobutanoate + 7,8-Diaminononanoate
2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone + S-Adenosylmethionine > Hydrogen ion + Ubiquinol-8 + S-Adenosylhomocysteine
Coproporphyrinogen III + S-Adenosylmethionine > Protoporphyrinogen IX + Carbon dioxide + L-Methionine + 5'-Deoxyadenosine
L-Homocysteine + S-Adenosylmethionine Hydrogen ion + L-Methionine + S-Adenosylhomocysteine
5-Aminoimidazole ribonucleotide + S-Adenosylmethionine 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + carbon monoxide + Hydrogen ion
S-Adenosylmethionine + Ribonuc-tri-P-reductases-inactive <> 5'-Deoxyadenosine + L-Methionine + Ribonuc-tri-P-reductases-active
L-Tyrosine + S-Adenosylmethionine + a reduced electron acceptor > Dehydroglycine + p-Cresol + 5'-Deoxyadenosine + L-Methionine + an oxidized electron acceptor + Hydrogen ion
Malonyl-CoA + S-Adenosylmethionine > malonyl-CoA methyl ester + S-Adenosylhomocysteine
S-Adenosylmethionine + a demethylated methyl acceptor > S-Adenosylhomocysteine + a methylated methyl acceptor
trans-Aconitic acid + S-Adenosylmethionine > E-3-Carboxy-2-pentenedioate 6-methyl ester + S-Adenosylhomocysteine
N-6-isopentyl adenosine-37 tRNA + S-Adenosylmethionine + <i>S</i>-sulfanyl-[acceptor] 2-methylthio-N-6-isopentyl adenosine-37 tRNA + S-Adenosylhomocysteine + L-Methionine + 5'-Deoxyadenosine + an unsulfurated sulfur acceptor + Hydrogen ion
6-Carboxy-5,6,7,8-tetrahydropterin + S-Adenosylmethionine + Hydrogen ion > 7-carboxy-7-deazaguanine + 5'-Deoxyadenosine + L-Methionine + Ammonia
a guanine<sup>1516</sup> in 16S rRNA + S-Adenosylmethionine > an <i>N</i><sup>2</sup>-methylguanine<sup>1516</sup> in 16S rRNA + S-Adenosylhomocysteine + Hydrogen ion
guanine<sup>2069</sup> in 23S rRNA + S-Adenosylmethionine > N<sup>7</sup>-methylguanine<sup>2069</sup> in 23S rRNA + S-Adenosylhomocysteine
Adenosine triphosphate + L-Methionine + Water > Phosphate + Pyrophosphate + S-Adenosylmethionine
Hydrogen ion + S-Adenosylmethionine > Carbon dioxide + S-Adenosylmethioninamine
S-Adenosylmethionine <> S-Adenosylhomocysteine
S-Adenosylmethionine + trans-Aconitic acid <> S-Adenosylhomocysteine + E-3-Carboxy-2-pentenedioate 6-methyl ester
S-Adenosylmethionine + Phospholipid olefinic fatty acid <> S-Adenosylhomocysteine + Phospholipid cyclopropane fatty acid
S-Adenosylmethionine + tRNA containing 5-aminomethyl-2-thiouridine <> S-Adenosylhomocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate
S-Adenosylmethionine + DNA adenine <> S-Adenosylhomocysteine + DNA 6-methylaminopurine
2 S-Adenosylmethionine + Uroporphyrinogen III + Precorrin-1 <>2 S-Adenosylhomocysteine + Precorrin 2
2 S-Adenosylmethionine <> S-Adenosylhomocysteine +2 L-Methionine + 5'-Deoxyadenosine
2 S-Adenosylmethionine + Reduced acceptor <> S-Adenosylhomocysteine +2 L-Methionine + 5'-Deoxyadenosine
S-Adenosylmethionine + Protein glutamate <> S-Adenosylhomocysteine + Protein glutamate methyl ester
S-Adenosylmethionine <> S-Adenosylhomocysteine + DNA 5-methylcytosine
S-Adenosylmethionine <> S-Adenosylhomocysteine
S-Adenosylmethionine + Protein L-isoaspartate <> S-Adenosylhomocysteine + Protein L-isoaspartate methyl ester
S-Adenosylmethionine <> S-Adenosylhomocysteine
S-Adenosylmethionine <> S-Adenosylhomocysteine
L-Tyrosine + S-Adenosylmethionine + NADPH <> 2-iminoacetate + p-Cresol + 5'-Deoxyadenosine + L-Methionine + NADP + Hydrogen ion
S-Adenosylmethionine + tRNA <> S-Adenosylhomocysteine + tRNA containing N6-methyladenine
More...

SMPDB Pathways:
Biotin metabolismPW000762 Pw000762Pw000762 greyscalePw000762 simple
Lipoic acid metabolismPW000770 Pw000770Pw000770 greyscalePw000770 simple
KEGG Pathways:
EcoCyc Pathways:
Concentrations
ConcentrationStrainMediaGrowth StatusGrowth SystemTemperatureDetails
184± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucoseMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
1100± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerolMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
388± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetateMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
44± 0 uMBW2511348 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L GlucoStationary Phase, glucose limitedBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h37 oCPMID: 17379776
Find out more about how we convert literature concentrations.
Spectra
Spectra:Not Available
References
References:
  • Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. Pubmed: 19561621
  • Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. Pubmed: 17379776
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
  • Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. Pubmed: 18331064
Synthesis Reference:Lin, 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)
External Links:
ResourceLink
CHEBI ID15414
HMDB IDHMDB01185
Pubchem Compound ID1079
Kegg IDC00019
ChemSpider ID21169292
WikipediaS-Adenosylmethionine
BioCyc IDS-ADENOSYLMETHIONINE
EcoCyc IDS-ADENOSYLMETHIONINE

Enzymes

General function:
Coenzyme transport and metabolism
Specific function:
S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1
Gene Name:
hemX
Uniprot ID:
P09127
Molecular weight:
42963
Reactions
S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.
S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.
General function:
Involved in protein-L-isoaspartate (D-aspartate) O-methyltransferase activity
Specific function:
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. This enzyme does not act on D-aspartyl residues
Gene Name:
pcm
Uniprot ID:
P0A7A5
Molecular weight:
23258
Reactions
S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester.
General function:
Involved in adenosylmethionine decarboxylase activity
Specific function:
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine
Gene Name:
speD
Uniprot ID:
P0A7F6
Molecular weight:
30384
Reactions
S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2).
General function:
Involved in methionine adenosyltransferase activity
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. Is essential for growth
Gene Name:
metK
Uniprot ID:
P0A817
Molecular weight:
41951
Reactions
ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L-methionine.
General function:
Involved in RNA binding
Specific function:
Specifically methylates guanosine-37 in various tRNAs
Gene Name:
trmD
Uniprot ID:
P0A873
Molecular weight:
28422
Reactions
S-adenosyl-L-methionine + guanine(37) in tRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA.
General function:
Involved in lipid biosynthetic process
Specific function:
Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge
Gene Name:
cfa
Uniprot ID:
P0A9H7
Molecular weight:
43909
Reactions
S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.
General function:
Involved in catalytic activity
Specific function:
Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine
Gene Name:
pflA
Uniprot ID:
P0A9N4
Molecular weight:
28204
Reactions
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.
General function:
Involved in [formate-C-acetyltransferase]-activating enzyme activity
Specific function:
Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine
Gene Name:
nrdG
Uniprot ID:
P0A9N8
Molecular weight:
17446
General function:
Involved in nucleic acid binding
Specific function:
Specifically methylates the guanosine in position 966 of 16S rRNA in the assembled 30S particle
Gene Name:
rsmD
Uniprot ID:
P0ADX9
Molecular weight:
21677
Reactions
S-adenosyl-L-methionine + guanosine(966) in 16S rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanosine(966) in 16S rRNA.
General function:
Involved in methyltransferase activity
Specific function:
Multifunctional enzyme that catalyzes the SAM-dependent methylation of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 and then position C-12 or C-18 to form trimethylpyrrocorphin 2. It also catalyzes the conversion of precorrin-2 into siroheme. This reaction consists of the NAD- dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme
Gene Name:
cysG
Uniprot ID:
P0AEA8
Molecular weight:
49951
Reactions
S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.
S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.
Precorrin-2 + NAD(+) = sirohydrochlorin + NADH.
Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+).
General function:
Involved in DNA binding
Specific function:
This methylase recognizes the double-stranded sequence CCWGG, causes specific methylation on C-2 on both strands
Gene Name:
dcm
Uniprot ID:
P0AED9
Molecular weight:
53464
Reactions
S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
General function:
Involved in transaminase activity
Specific function:
Catalyzes the transfer of the alpha-amino group from S- adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor
Gene Name:
bioA
Uniprot ID:
P12995
Molecular weight:
47335
Reactions
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate.
General function:
Involved in catalytic activity
Specific function:
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical- based mechanism
Gene Name:
bioB
Uniprot ID:
P12996
Molecular weight:
38648
Reactions
Dethiobiotin + sulfur + 2 S-adenosyl-L-methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosine.
General function:
Involved in 2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity
Specific function:
S-adenosyl-L-methionine + 3- demethylubiquinone-9 = S-adenosyl-L-homocysteine + ubiquinone-9
Gene Name:
ubiG
Uniprot ID:
P17993
Molecular weight:
26555
Reactions
S-adenosyl-L-methionine + 3-demethylubiquinone-n = S-adenosyl-L-homocysteine + ubiquinone-n.
S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol = S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol.
General function:
Involved in coproporphyrinogen oxidase activity
Specific function:
Anaerobic transformation of coproporphyrinogen-III into protoporphyrinogen-IX
Gene Name:
hemN
Uniprot ID:
P32131
Molecular weight:
52729
Reactions
Coproporphyrinogen-III + 2 S-adenosyl-L-methionine = protoporphyrinogen-IX + 2 CO(2) + 2 L-methionine + 2 5'-deoxyadenosine.
General function:
Involved in iron-sulfur cluster binding
Specific function:
Activation of pyruvate formate-lyase 2 under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine
Gene Name:
pflC
Uniprot ID:
P32675
Molecular weight:
32429
Reactions
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.
General function:
Involved in methyltransferase activity
Specific function:
Specifically methylates the guanosine in position 745 of 23S rRNA
Gene Name:
rlmA
Uniprot ID:
P36999
Molecular weight:
30419
Reactions
S-adenosyl-L-methionine + guanine(745) in 23S rRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(745) in 23S rRNA.
General function:
Involved in nucleic acid binding
Specific function:
S-adenosyl-L-methionine + DNA adenine = S- adenosyl-L-homocysteine + DNA 6-methylaminopurine
Gene Name:
yfcB
Uniprot ID:
P39199
Molecular weight:
35001
Reactions
S-adenosyl-L-methionine + glutamine in ribosomal protein L3 = S-adenosyl-L-homocysteine + N5-methylglutamine in ribosomal protein L3.
General function:
Involved in nucleic acid binding
Specific function:
Specifically methylates the guanosine in position 1207 of 16S rRNA in the 30S particle
Gene Name:
rsmC
Uniprot ID:
P39406
Molecular weight:
37624
Reactions
S-adenosyl-L-methionine + guanosine(1207) in 16S rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanosine(1207) in 16S rRNA.
General function:
Involved in nucleic acid binding
Specific function:
Specifically methylates the guanosine in position 1835 (m2G1835) of 23S rRNA
Gene Name:
rlmG
Uniprot ID:
P42596
Molecular weight:
42331
Reactions
S-adenosyl-L-methionine + guanosine(1835) in 23S rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanosine(1835) in 23S rRNA.
General function:
Involved in coproporphyrinogen oxidase activity
Specific function:
Not Available
Gene Name:
yggW
Uniprot ID:
P52062
Molecular weight:
42584
General function:
Involved in catalytic activity
Specific function:
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. Free octanoate is not a substrate for lipA
Gene Name:
lipA
Uniprot ID:
P60716
Molecular weight:
36071
Reactions
Protein N(6)-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine.
General function:
Involved in rRNA (adenine-N6-)-methyltransferase activity
Specific function:
Specifically methylates the adenine in position 1618 of 23S rRNA
Gene Name:
rlmF
Uniprot ID:
P75782
Molecular weight:
34226
Reactions
S-adenosyl-L-methionine + adenine(1618) in 23S rRNA = S-adenosyl-L-homocysteine + rRNA containing N(6)-methyladenine(1618) in 23S rRNA.
General function:
Involved in oxidoreductase activity
Specific function:
Activation of pyruvate formate-lyase 2 under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine
Gene Name:
ybiY
Uniprot ID:
P75794
Molecular weight:
33038
Reactions
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.
General function:
Involved in trans-aconitate 2-methyltransferase activity
Specific function:
Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate at high affinity and of cis- aconitate, isocitrate, and citrate at lower velocities and affinities
Gene Name:
tam
Uniprot ID:
P76145
Molecular weight:
29006
Reactions
S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-3-(methoxycarbonyl)pent-2-enedioate.
General function:
Involved in homocysteine S-methyltransferase activity
Specific function:
Catalyzes methyl transfer from S-methylmethionine or S- adenosylmethionine (less efficient) to homocysteine, selenohomocysteine and less efficiently selenocysteine
Gene Name:
mmuM
Uniprot ID:
Q47690
Molecular weight:
33422
Reactions
S-methyl-L-methionine + L-homocysteine = 2 L-methionine.
General function:
Involved in catalytic activity
Specific function:
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5- phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S
Gene Name:
thiG
Uniprot ID:
P30139
Molecular weight:
26896
Reactions
1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS] = 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H(2)O.
General function:
Involved in catalytic activity
Specific function:
Catalyzes the radical-mediated cleavage of tyrosine to dehydroglycine and p-cresol
Gene Name:
thiH
Uniprot ID:
P30140
Molecular weight:
43320
Reactions
L-tyrosine + S-adenosyl-L-methionine + reduced acceptor = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + acceptor + 2 H(+).
General function:
Involved in thiamine biosynthetic process
Specific function:
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction
Gene Name:
thiC
Uniprot ID:
P30136
Molecular weight:
70850
Reactions
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO.
General function:
Involved in methyltransferase activity
Specific function:
Methyltransferase required for the conversion of dimethylmenaquinone (DMKH2) to menaquinone (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2)
Gene Name:
ubiE
Uniprot ID:
P0A887
Molecular weight:
28073
Reactions
A demethylmenaquinone + S-adenosyl-L-methionine = a menaquinol + S-adenosyl-L-homocysteine.
S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol = S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol.
General function:
Involved in biotin biosynthetic process
Specific function:
BioC is involved in an early, but chemically unexplored, step in the conversion of pimelic acid to biotin
Gene Name:
bioC
Uniprot ID:
P12999
Molecular weight:
28276
Reactions
S-adenosyl-L-methionine + malonyl-CoA = S-adenosyl-L-homocysteine + malonyl-CoA methyl ester.
General function:
Not Available
Specific function:
Not Available
Gene Name:
rlmL
Uniprot ID:
P75864
Molecular weight:
Not Available
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Methylates the translation termination release factor RF1/PrfA on 'Gln-235' and RF2/PrfB on 'Gln-252'
Gene Name:
hemK
Uniprot ID:
P0ACC1
Molecular weight:
30975
Reactions
S-adenosyl-L-methionine + glutamine in release factor = S-adenosyl-L-homocysteine + N5-methylglutamine in release factor.
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. Has also a DNA glycosylase/AP lyase activity that removes C mispaired with oxidized T from DNA, and may play a role in protection of DNA against oxidative stress
Gene Name:
rsmA
Uniprot ID:
P06992
Molecular weight:
30420
Reactions
4 S-adenosyl-L-methionine + adenine(1518)/adenine(1519) in 16S rRNA = 4 S-adenosyl-L-homocysteine + N(6)-dimethyladenine(1518)/N(6)-dimethyladenine(1519) in 16S rRNA.
General function:
tRNA methylthiolation
Specific function:
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Gene Name:
miaB
Uniprot ID:
P0AEI1
Molecular weight:
53662
Reactions
N(6)-dimethylallyladenine(37) in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = 2-methylthio-N(6)-dimethylallyladenine(37) in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
General function:
RNA modification
Specific function:
Catalyzes the methylthiolation of the residue Asp-89 of ribosomal protein S12.
Gene Name:
rimO
Uniprot ID:
P0AEI4
Molecular weight:
49581
Reactions
L-aspartate-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = 3-methylthio-L-aspartate-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine