Record Information
Version2.0
Creation Date2012-05-31 13:02:20 -0600
Update Date2015-09-13 12:56:09 -0600
Secondary Accession Numbers
  • ECMDB00939
Identification
Name:S-Adenosylhomocysteine
Description:S-Adenosylhomocysteine (AdoHcy) is the immediate precursor of homocysteine. The reaction is catalyzed by S-adenosylhomocysteine hydrolase and is reversible with the equilibrium favoring formation of AdoHcy. 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, AdoHcy is the product of all methylation reactions that involve S-adenosylmethionine (AdoMet) as the methyl donor.
Structure
Thumb
Synonyms:
  • (S)-5'-(S)-(3-Amino-3-carboxypropyl)-5'-thioadenosine
  • 2-S-adenosyl-L-homocysteine
  • 2-S-Adenosyl-L-homocysteine
  • 5'-Deoxy-S-adenosyl-L-homocysteine
  • 5'-S-(3-Amino-3-carboxypropyl)-5'-thio-L-Adenosine
  • S-adenosyl-homocysteine
  • S-adenosylhomocysteine
  • Adenosyl-homo-CYS
  • Adenosyl-L-homocysteine
  • Adenosylhomo-CYS
  • Adenosylhomocysteine
  • Adohcy
  • Formycinylhomocysteine
  • L-5'-S-(3-Amino-3-carboxypropyl)-5'-thior-Adenosine
  • L-S-Adenosyl-Homocysteine
  • L-S-Adenosylhomocysteine
  • S-(5'-Adenosyl)-L-homocysteine
  • S-(5'-Deoxyadenosin-5'-yl)-L-homocysteine
  • S-(5'-Deoxyadenosine-5')-L-homocysteine
  • S-Adenosyl-homocysteine
  • S-Adenosyl-L-homocysteine
  • S-adenosylhomocysteine
  • SAH
  • SAHC
Chemical Formula:C14H20N6O5S
Weight:Average: 384.411
Monoisotopic: 384.12158847
InChI Key:ZJUKTBDSGOFHSH-WFMPWKQPSA-N
InChI: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
CAS number:979-92-0
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 IUPAC Name:S-adenosyl-L-homocysteine
SMILES:N[C@@H](CCSC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC2=C(N)N=CN=C12)C(O)=O
Chemical Taxonomy
Description 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
Physical Properties
State:Solid
Charge:0
Melting point:209-211 °C
Experimental Properties:
PropertyValueSource
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
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
2 S-Adenosylmethionine + Uroporphyrinogen III >2 S-Adenosylhomocysteine + Precorrin 2 + Hydrogen ion
S-Adenosylhomocysteine + Water <> Adenine + S-Ribosyl-L-homocysteine
S-Adenosylmethionine + L-Homocysteine + S-Methylmethionine <> S-Adenosylhomocysteine + 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
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
S-Adenosylhomocysteine + Water <> S-Ribosyl-L-homocysteine + Adenine
S-Adenosylmethionine + L-Homocysteine <> S-Adenosylhomocysteine + L-Methionine
2 S-Adenosylmethionine + Uroporphyrinogen III <>2 S-Adenosylhomocysteine + Precorrin 2
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
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
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
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
S-Ribosyl-L-homocysteine + Adenine < S-Adenosylhomocysteine + Water
2-Demethylmenaquinol 8 + S-Adenosylmethionine > Menaquinol 8 + Hydrogen ion + S-Adenosylhomocysteine
2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone + S-Adenosylmethionine > Hydrogen ion + Ubiquinol-8 + S-Adenosylhomocysteine
L-Homocysteine + S-Adenosylmethionine Hydrogen ion + L-Methionine + S-Adenosylhomocysteine
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
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
S-adenosyl-L-methionine + Malonyl-CoA > S-Adenosylhomocysteine + malonyl-CoA methyl ester
S-adenosyl-L-methionine + phospholipid olefinic fatty acid > S-Adenosylhomocysteine + phospholipid cyclopropane fatty acid
S-adenosyl-L-methionine + protein L-glutamate > S-Adenosylhomocysteine + protein L-glutamate methyl ester
S-adenosyl-L-methionine + Uroporphyrinogen III > S-Adenosylhomocysteine + Precorrin-1
S-adenosyl-L-methionine + Precorrin-1 > S-Adenosylhomocysteine + Precorrin-2
S-adenosyl-L-methionine + DNA > S-Adenosylhomocysteine + DNA containing 5-methylcytosine
S-adenosyl-L-methionine + DNA adenine > S-Adenosylhomocysteine + DNA 6-methylaminopurine
S-adenosyl-L-methionine + Uroporphyrinogen III > S-Adenosylhomocysteine + Precorrin-1
S-adenosyl-L-methionine + Precorrin-1 > S-Adenosylhomocysteine + Precorrin-2
S-adenosyl-L-methionine + tRNA > S-Adenosylhomocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate
S-Adenosylhomocysteine + Water > S-Ribosyl-L-homocysteine + Adenine
S-adenosyl-L-methionine + protein L-isoaspartate > S-Adenosylhomocysteine + protein L-isoaspartate alpha-methyl ester
S-adenosyl-L-methionine + glutamine in ribosomal protein L3 > S-Adenosylhomocysteine + N5-methylglutamine in ribosomal protein L3
S-adenosyl-L-methionine + glutamine in release factor > S-Adenosylhomocysteine + N5-methylglutamine in release factor
S-adenosyl-L-methionine + guanine(745) in 23S rRNA > S-Adenosylhomocysteine + N(1)-methylguanine(745) in 23S rRNA
S-adenosyl-L-methionine + guanosine(2251) in 23S rRNA > S-Adenosylhomocysteine + 2'-O-methylguanosine(2251) in 23S rRNA
S-adenosyl-L-methionine + uracil(747) in 23S rRNA > S-Adenosylhomocysteine + 5-methyluracil(747) in 23S rRNA
S-adenosyl-L-methionine + uracil(1939) in 23S rRNA > S-Adenosylhomocysteine + 5-methyluracil(1939) in 23S rRNA
S-adenosyl-L-methionine + uridine(2552) in 23S rRNA > S-Adenosylhomocysteine + 2'-O-methyluridine(2552) in 23S rRNA
S-adenosyl-L-methionine + adenine(1618) in 23S rRNA > S-Adenosylhomocysteine + rRNA containing N(6)-methyladenine(1618) in 23S rRNA
S-adenosyl-L-methionine + guanine(1835) in 23S rRNA > S-Adenosylhomocysteine + N(2)-methylguanine(1835) in 23S rRNA
S-adenosyl-L-methionine + rRNA > S-Adenosylhomocysteine + rRNA containing N3-methylpseudouridine
S-adenosyl-L-methionine + pseudouridine(1915) in 23S rRNA > S-Adenosylhomocysteine + N(3)-methylpseudouridine(1915) in 23S rRNA
S-adenosyl-L-methionine + cytosine(1962) in 23S rRNA > S-Adenosylhomocysteine + 5-methylcytosine(1962) in 23S rRNA
S-adenosyl-L-methionine + guanine(2445) in 23S rRNA > S-Adenosylhomocysteine + N(2)-methylguanine(2445) in 23S rRNA
S-adenosyl-L-methionine + cytidine(2498) in 23S rRNA > S-Adenosylhomocysteine + 2'-O-methylcytidine(2498) in 23S rRNA
2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA > S-Adenosylhomocysteine + L-Methionine + 5'-Deoxyadenosine + 2-methyladenine(2503) in 23S rRNA
4 S-adenosyl-L-methionine + adenine(1518)/adenine(1519) in 16S rRNA >4 S-Adenosylhomocysteine + N(6)-dimethyladenine(1518)/N(6)-dimethyladenine(1519) in 16S rRNA
S-adenosyl-L-methionine + cytosine(967) in 16S rRNA > S-Adenosylhomocysteine + 5-methylcytosine(967) in 16S rRNA
S-adenosyl-L-methionine + guanine(1207) in 16S rRNA > S-Adenosylhomocysteine + N(2)-methylguanine(1207) in 16S rRNA
S-adenosyl-L-methionine + guanine(966) in 16S rRNA > S-Adenosylhomocysteine + N(2)-methylguanine(966) in 16S rRNA
S-adenosyl-L-methionine + uracil(1498) in 16S rRNA > S-Adenosylhomocysteine + N(3)-methyluracil(1498) in 16S rRNA
S-adenosyl-L-methionine + cytosine(1407) in 16S rRNA > S-Adenosylhomocysteine + 5-methylcytosine(1407) in 16S rRNA
S-adenosyl-L-methionine + guanine(527) in 16S rRNA > S-Adenosylhomocysteine + N(7)-methylguanine(527) in 16S rRNA
S-adenosyl-L-methionine + cytosine(1402) in 16S rRNA > S-Adenosylhomocysteine + N(4)-methylcytosine(1402) in 16S rRNA
S-adenosyl-L-methionine + cytidine(1402) in 16S rRNA > S-Adenosylhomocysteine + 2'-O-methylcytidine(1402) in 16S rRNA
S-adenosyl-L-methionine + guanine(1516) in 16S rRNA > S-Adenosylhomocysteine + N(2)-methylguanine(1516) in 16S rRNA
S-adenosyl-L-methionine + DNA adenine > S-Adenosylhomocysteine + DNA 6-methylaminopurine
S-adenosyl-L-methionine + trans-Aconitic acid > S-Adenosylhomocysteine + (E)-3-(Methoxycarbonyl)pent-2-enedioate
S-adenosyl-L-methionine + uridine(54) in tRNA > S-Adenosylhomocysteine + 5-methyluridine(54) in tRNA
S-adenosyl-L-methionine + guanine(46) in tRNA > S-Adenosylhomocysteine + N(7)-methylguanine(46) in tRNA
S-adenosyl-L-methionine + guanine(37) in tRNA > S-Adenosylhomocysteine + N(1)-methylguanine(37) in tRNA
S-adenosyl-L-methionine + guanosine(18) in tRNA > S-Adenosylhomocysteine + 2'-O-methylguanosine(18) in tRNA
S-adenosyl-L-methionine + cytidine(32) in tRNA > S-Adenosylhomocysteine + 2'-O-methylcytidine(32) in tRNA
S-adenosyl-L-methionine + uridine(32) in tRNA > S-Adenosylhomocysteine + 2'-O-methyluridine(32) in tRNA
S-adenosyl-L-methionine + cytidine(34) in tRNA > S-Adenosylhomocysteine + 2'-O-methylcytidine(34) in tRNA
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine(34) in tRNA(Leu) > S-Adenosylhomocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine(34) in tRNA(Leu)
S-adenosyl-L-methionine + adenine(37) in tRNA(1)(Val) > S-Adenosylhomocysteine + N(6)-methyladenine(37) in tRNA(1)(Val)
A demethylmenaquinone + S-adenosyl-L-methionine > Menaquinol 6 + S-Adenosylhomocysteine
S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol > S-Adenosylhomocysteine + 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol
S-adenosyl-L-methionine + 3-demethylubiquinone-n > S-Adenosylhomocysteine + ubiquinone-n
S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol > S-Adenosylhomocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol
S-adenosyl-L-methionine + DNA adenine > S-Adenosylhomocysteine + DNA 6-methylaminopurine
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
S-Adenosylmethionine + tRNA <> S-Adenosylhomocysteine + tRNA containing N6-methyladenine
S-Adenosylhomocysteine + Water > Adenine + S-ribosyl-L-homocysteine + S-ribosyl-L-homocysteine
a malonyl-[acp] + S-adenosyl-L-methionine > S-Adenosylhomocysteine + a malonyl-[acp] methyl ester
Uroporphyrinogen III + S-adenosyl-L-methionine > Hydrogen ion + S-Adenosylhomocysteine + Precorrin-1
Precorrin-1 + S-adenosyl-L-methionine > Precorrin-2 + S-Adenosylhomocysteine
2-Octaprenyl-6-hydroxyphenol + S-adenosyl-L-methionine + 2-Octaprenyl-6-hydroxyphenol > Hydrogen ion + S-Adenosylhomocysteine + 2-methoxy-6-(all-trans-octaprenyl)phenol
3-demethylubiquinol-8 + S-adenosyl-L-methionine > Hydrogen ion + S-Adenosylhomocysteine + Ubiquinol 8 + Ubiquinol-8
2-Octaprenyl-6-methoxy-1,4-benzoquinol + S-adenosyl-L-methionine > S-Adenosylhomocysteine + Hydrogen ion + 6-Methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol
2-Demethylmenaquinol 8 + S-adenosyl-L-methionine > Hydrogen ion + S-Adenosylhomocysteine + Menaquinol 8
S-Adenosylhomocysteine + Water > Adenine
2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine > S-Adenosylhomocysteine + Ubiquinol-8 + Hydrogen ion
2-Octaprenyl-6-methoxy-1,4-benzoquinol + S-adenosyl-L-methionine > 2-Octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol + S-Adenosylhomocysteine + Hydrogen ion
a [phospholipid] olefinic fatty acid + S-adenosyl-L-methionine > a [phospholipid] cyclopropane fatty acid + S-Adenosylhomocysteine + Hydrogen ion
More...

SMPDB Pathways:
Biotin metabolismPW000762 ThumbThumb?image type=greyscaleThumb?image type=simple
Cyclopropane Fatty Acid (CFA) BiosynthesisPW002109 ThumbThumb?image type=greyscaleThumb?image type=simple
Menaquinol biosythesisPW001897 ThumbThumb?image type=greyscaleThumb?image type=simple
Porphyrin metabolismPW000936 ThumbThumb?image type=greyscaleThumb?image type=simple
Quorum SensingPW000836 ThumbThumb?image type=greyscaleThumb?image type=simple
S-adenosyl-L-methionine cyclePW002080 ThumbThumb?image type=greyscaleThumb?image type=simple
Secondary Metabolites: Ubiquinol biosynthesisPW000981 ThumbThumb?image type=greyscaleThumb?image type=simple
Secondary Metabolites: Ubiquinol biosynthesis 2PW002036 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways:
EcoCyc Pathways:
Concentrations
Not Available
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
References
References:
  • 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
  • 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
  • Fowler B: Homocysteine: overview of biochemistry, molecular biology, and role in disease processes. Semin Vasc Med. 2005 May;5(2):77-86. Pubmed: 16047261
  • 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
  • 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
  • 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
  • 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
  • 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
  • Metz J: Cobalamin deficiency and the pathogenesis of nervous system disease. Annu Rev Nutr. 1992;12:59-79. Pubmed: 1354465
  • Miller AL: The methionine-homocysteine cycle and its effects on cognitive diseases. Altern Med Rev. 2003 Feb;8(1):7-19. Pubmed: 12611557
  • 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
  • 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
  • Palella TD, Schatz RA, Wilens TE, Fox IH: S-Adenosylhomocysteine accumulation and selective cytotoxicity in cultured J Lab Clin Med. 1982 Aug;100(2):269-78. Pubmed: 6980250
  • 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. Pubmed: 19212411
  • 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
  • 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
  • van Guldener C, Stehouwer CD: Homocysteine and methionine metabolism in renal failure. Semin Vasc Med. 2005 May;5(2):201-8. Pubmed: 16047272
  • 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
  • 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
  • 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
  • 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:Holy, 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)
External Links:
ResourceLink
CHEBI ID16680
HMDB IDHMDB00939
Pubchem Compound ID439155
Kegg IDC00021
ChemSpider ID388301
WikipediaSAH
BioCyc IDADENOSYL-HOMO-CYS
EcoCyc IDADENOSYL-HOMO-CYS
Ligand ExpoSAH

Enzymes

General function:
Involved in S-adenosylmethionine-dependent methyltransferase activity
Specific function:
Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP
Gene Name:
cheR
Uniprot ID:
P07364
Molecular weight:
32849
Reactions
S-adenosyl-L-methionine + protein L-glutamate = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester.
General function:
Involved in site-specific DNA-methyltransferase (adenine-specific) activity
Specific function:
The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'
Gene Name:
hsdM
Uniprot ID:
P08957
Molecular weight:
59306
Reactions
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.
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 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 tRNA (guanine-N7-)-methyltransferase activity
Specific function:
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA
Gene Name:
trmB
Uniprot ID:
P0A8I5
Molecular weight:
27307
Reactions
S-adenosyl-L-methionine + guanine(46) in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) 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 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 site-specific DNA-methyltransferase (adenine-specific) activity
Specific function:
Methylates DNA within the sequence GATC and protects the DNA from cleavage by the restriction endonuclease MboI. Although it shares sequence specificity with a number of type II restriction endonucleases and methylases, it is thought to act in postreplication mismatch repair rather than as a part of a restriction modification system. May also play a role in DNA replication
Gene Name:
dam
Uniprot ID:
P0AEE8
Molecular weight:
32099
Reactions
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.
General function:
Involved in adenosylhomocysteine nucleosidase activity
Specific function:
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S- adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Can also use 5'-isobutylthioadenosine, 5'-n- butylthioadenosine, S-adenosyl-D-homocysteine, decarboxylated adenosylhomocysteine, deaminated adenosylhomocysteine and S-2-aza- adenosylhomocysteine as substrates
Gene Name:
mtnN
Uniprot ID:
P0AF12
Molecular weight:
24354
Reactions
S-adenosyl-L-homocysteine + H(2)O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine.
S-methyl-5'-thioadenosine + H(2)O = S-methyl-5-thio-D-ribose + adenine.
General function:
Involved in tRNA (guanosine-2'-O-)-methyltransferase activity
Specific function:
Specifically methylates guanosine-18 in various tRNAs
Gene Name:
trmH
Uniprot ID:
P0AGJ2
Molecular weight:
25343
Reactions
S-adenosyl-L-methionine + guanosine(18) in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine(18) in tRNA.
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 tRNA (uracil-5-)-methyltransferase activity
Specific function:
Catalyzes the formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs
Gene Name:
trmA
Uniprot ID:
P23003
Molecular weight:
41967
Reactions
S-adenosyl-L-methionine + uridine(54) in tRNA = S-adenosyl-L-homocysteine + 5-methyluridine(54) in tRNA.
General function:
Involved in DNA binding
Specific function:
S-adenosyl-L-methionine + DNA adenine = S- adenosyl-L-homocysteine + DNA 6-methylaminopurine
Gene Name:
yhdJ
Uniprot ID:
P28638
Molecular weight:
33397
Reactions
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.
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 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 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 oxidoreductase activity
Specific function:
Catalyzes the last two steps in the biosynthesis of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34
Gene Name:
mnmC
Uniprot ID:
P77182
Molecular weight:
74434
Reactions
S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate.
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 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 methylates the ribose of guanosine 2251 in 23S rRNA
Gene Name:
rlmB
Uniprot ID:
P63177
Molecular weight:
26556
Reactions
S-adenosyl-L-methionine + guanosine(2251) in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine(2251) in 23S rRNA.
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Catalyzes the formation of 5-methyl-uridine at position 747 (M-5-U747) in 23S rRNA
Gene Name:
rumB
Uniprot ID:
P75817
Molecular weight:
41955
Reactions
S-adenosyl-L-methionine + uracil(747) in 23S rRNA = S-adenosyl-L-homocysteine + 5-methyluracil(747) in 23S rRNA.
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Catalyzes the formation of 5-methyl-uridine at position 1939 (M-5-U1939) in 23S rRNA
Gene Name:
rumA
Uniprot ID:
P55135
Molecular weight:
48052
Reactions
S-adenosyl-L-methionine + uracil(1939) in 23S rRNA = S-adenosyl-L-homocysteine + 5-methyluracil(1939) in 23S rRNA.
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit
Gene Name:
rlmE
Uniprot ID:
P0C0R7
Molecular weight:
23335
Reactions
S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine(2552) in 23S rRNA.
General function:
Involved in protein homodimerization activity
Specific function:
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. Specific for fully assembled 70S ribosomes
Gene Name:
rlmH
Uniprot ID:
P0A8I8
Molecular weight:
17341
Reactions
S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing N3-methylpseudouridine.
S-adenosyl-L-methionine + pseudouridine(1915) in 23S rRNA = S-adenosyl-L-homocysteine + N(3)-methylpseudouridine(1915) in 23S rRNA.
General function:
Involved in RNA binding
Specific function:
Specifically methylates the cytosine at position 1962 (m5C1962) of 23S rRNA. Methylation occurs before assembly of 23S rRNA into 50S subunits
Gene Name:
rlmI
Uniprot ID:
P75876
Molecular weight:
44357
Reactions
S-adenosyl-L-methionine + cytosine(1962) in 23S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(1962) in 23S rRNA.
General function:
Involved in nucleic acid binding
Specific function:
Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA. Modifies C2498 in naked 23S rRNA, but not in assembled 50S subunits or ribosomes
Gene Name:
rlmM
Uniprot ID:
P0ADR6
Molecular weight:
41905
Reactions
S-adenosyl-L-methionine + cytidine(2498) in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(2498) in 23S rRNA.
General function:
Involved in 4 iron, 4 sulfur cluster binding
Specific function:
Specifically methylates position 2 of adenine 2503 in 23S rRNA
Gene Name:
rlmN
Uniprot ID:
P36979
Molecular weight:
43085
Reactions
2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(2503) in 23S rRNA.
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:
Defense mechanisms
Specific function:
Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA
Gene Name:
rsmB
Uniprot ID:
P36929
Molecular weight:
48347
Reactions
S-adenosyl-L-methionine + cytosine(967) in 16S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(967) in 16S rRNA.
General function:
Involved in rRNA (uridine-N3-)-methyltransferase activity
Specific function:
Specifically methylates the uridine in position 1498 of 16S rRNA in the fully assembled 30S ribosomal subunit
Gene Name:
rsmE
Uniprot ID:
P0AGL7
Molecular weight:
26978
Reactions
S-adenosyl-L-methionine + uracil(1498) in 16S rRNA = S-adenosyl-L-homocysteine + N(3)-methyluracil(1498) in 16S rRNA.
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Specifically methylates the cytosine at position 1407 (m5C1407) of 16S rRNA
Gene Name:
rsmF
Uniprot ID:
P76273
Molecular weight:
53227
Reactions
S-adenosyl-L-methionine + cytosine(1407) in 16S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(1407) in 16S rRNA.
General function:
Cell wall/membrane/envelope biogenesis
Specific function:
Specifically methylates the N7 position of guanosine in position 527 of 16S rRNA
Gene Name:
rsmG
Uniprot ID:
P0A6U5
Molecular weight:
23431
Reactions
S-adenosyl-L-methionine + guanine(527) in 16S rRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(527) in 16S rRNA.
General function:
Cell wall/membrane/envelope biogenesis
Specific function:
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. In vitro, active on the assembled 30S subunit, but not naked 16S rRNA or 70S ribosomes
Gene Name:
rsmH
Uniprot ID:
P60390
Molecular weight:
34877
Reactions
S-adenosyl-L-methionine + cytosine(1402) in 16S rRNA = S-adenosyl-L-homocysteine + N(4)-methylcytosine(1402) in 16S rRNA.
General function:
Involved in protein binding
Specific function:
Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. In vitro, active on the assembled 30S subunit, but not naked 16S rRNA or 70S ribosomes
Gene Name:
rsmI
Uniprot ID:
P67087
Molecular weight:
31348
Reactions
S-adenosyl-L-methionine + cytidine(1402) in 16S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(1402) in 16S rRNA.
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Not Available
Gene Name:
yhiQ
Uniprot ID:
P68567
Molecular weight:
26949
Reactions
S-adenosyl-L-methionine + guanine(1516) in 16S rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanine(1516) in 16S rRNA.
General function:
Replication, recombination and repair
Specific function:
Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA
Gene Name:
trmJ
Uniprot ID:
P0AE01
Molecular weight:
27048
Reactions
S-adenosyl-L-methionine + cytidine(32) in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(32) in tRNA.
S-adenosyl-L-methionine + uridine(32) in tRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine(32) in tRNA.
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Not Available
Gene Name:
yibK
Uniprot ID:
P0AGJ7
Molecular weight:
17726
Reactions
S-adenosyl-L-methionine + cytidine(34) in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(34) in tRNA.
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine(34) in tRNA(Leu) = S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine(34) in tRNA(Leu).
General function:
Involved in nucleic acid binding
Specific function:
Specifically methylates the adenine in position 37 of tRNA(Val)
Gene Name:
yfiC
Uniprot ID:
P31825
Molecular weight:
27270
Reactions
S-adenosyl-L-methionine + adenine(37) in tRNA(1)(Val) = S-adenosyl-L-homocysteine + N(6)-methyladenine(37) in tRNA(1)(Val).
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