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Record Information
Creation Date2016-09-30 22:38:51 UTC
Update Date2020-05-21 16:29:03 UTC
Secondary Accession Numbers
  • BMDB00939
Metabolite Identification
Common NameS-Adenosylhomocysteine
DescriptionS-Adenosylhomocysteine, also known as adenosyl-homo-cys or adohcy, 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. S-Adenosylhomocysteine exists as a solid, possibly soluble (in water), and a very strong basic compound (based on its pKa) molecule. S-Adenosylhomocysteine exists in all living species, ranging from bacteria to humans. S-Adenosylhomocysteine is a potentially toxic compound.
(2S)-2-Amino-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}sulfanyl)butanoic acidChEBI
(2S)-2-Amino-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}sulphanyl)butanoic acidGenerator
Adenosylhomocysteine, SHMDB
S AdenosylhomocysteineHMDB
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
InChI Identifier
Chemical Taxonomy
Description belongs to the class of organic compounds known as gamma butyrolactones. Gamma butyrolactones are compounds containing a gamma butyrolactone moiety, which consists of an aliphatic five-member ring with four carbon atoms, one oxygen atom, and bears a ketone group on the carbon adjacent to the oxygen atom.
KingdomOrganic compounds
Super ClassOrganoheterocyclic compounds
Sub ClassGamma butyrolactones
Direct ParentGamma butyrolactones
Alternative Parents
  • Gamma butyrolactone
  • Tetrahydrofuran
  • Secondary alcohol
  • Carboxylic acid ester
  • 1,2-diol
  • Oxacycle
  • Monocarboxylic acid or derivatives
  • Carboxylic acid derivative
  • Organic oxygen compound
  • Organic oxide
  • Hydrocarbon derivative
  • Organooxygen compound
  • Carbonyl group
  • Alcohol
  • Aliphatic heteromonocyclic compound
Molecular FrameworkAliphatic heteromonocyclic compounds
External Descriptors
StatusDetected but not Quantified
  • Endogenous
  • Exogenous
BiofunctionNot Available
ApplicationNot Available
Cellular locations
  • Cytoplasm
  • Endoplasmic reticulum
  • Mitochondria
  • Myelin sheath
  • Nucleus
Physical Properties
Experimental Properties
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
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
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleYesChemAxon
Spectrum TypeDescriptionSplash Key
Biological Properties
Cellular Locations
  • Cytoplasm
  • Endoplasmic reticulum
  • Mitochondria
  • Myelin sheath
  • Nucleus
Biospecimen Locations
  • Kidney
  • Liver
  • Milk
  • Neuron
  • Placenta
  • Prostate Tissue
Normal Concentrations
KidneyExpected but not QuantifiedNot QuantifiedNot SpecifiedNot SpecifiedNormal
  • Not Applicable
LiverDetected but not QuantifiedNot QuantifiedNot SpecifiedNot Specified
MilkDetected but not QuantifiedNot QuantifiedNot SpecifiedNot Specified
NeuronExpected but not QuantifiedNot QuantifiedNot SpecifiedNot SpecifiedNormal
  • Not Applicable
PlacentaExpected but not QuantifiedNot QuantifiedNot SpecifiedNot SpecifiedNormal
  • Not Applicable
Prostate TissueExpected but not QuantifiedNot QuantifiedNot SpecifiedNot SpecifiedNormal
  • Not Applicable
Abnormal Concentrations
Not Available
DrugBank IDDB01752
Phenol Explorer Compound IDNot Available
FooDB IDFDB031150
KNApSAcK IDC00007230
Chemspider ID388301
KEGG Compound IDC00021
BiGG ID33543
Wikipedia LinkS-Adenosyl-L-homocysteine
PubChem Compound439155
PDB IDNot Available
ChEBI ID16680
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)Not Available
General References
  1. Mung D, Li L: Development of Chemical Isotope Labeling LC-MS for Milk Metabolomics: Comprehensive and Quantitative Profiling of the Amine/Phenol Submetabolome. Anal Chem. 2017 Apr 18;89(8):4435-4443. doi: 10.1021/acs.analchem.6b03737. Epub 2017 Mar 28. [PubMed:28306241 ]


General function:
Involved in phenylethanolamine N-methyltransferase acti
Specific function:
Converts noradrenaline to adrenaline.
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + Norepinephrine → S-Adenosylhomocysteine + Epinephrinedetails
Serotonin + S-Adenosylmethionine → N-Methylserotonin + S-Adenosylhomocysteinedetails
Tryptamine + S-Adenosylmethionine → N-Methyltryptamine + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + Niacinamide → S-Adenosylhomocysteine + 1-Methylnicotinamidedetails
General function:
Involved in histamine N-methyltransferase activity
Specific function:
Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine.
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + Histamine → S-Adenosylhomocysteine + 1-Methylhistaminedetails
General function:
Involved in histone-lysine N-methyltransferase activity
Specific function:
Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation (By similarity).
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Posttranslational modification, protein turnover, chaperones
Specific function:
Catalyzes the methyl esterification of L-isoaspartyl and D-aspartyl 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. Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin carboxyl-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in histone-lysine N-methyltransferase activity
Specific function:
Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Translation, ribosomal structure and biogenesis
Specific function:
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in histone-lysine N-methyltransferase activity
Specific function:
Putative histone methyltransferase that acts as a transcriptional repressor of smooth muscle gene expression. Promotes the transition from differentiated to proliferative smooth muscle by suppressing differentiation and maintaining the proliferative potential of vascular smooth muscle cells. Also plays a role in endothelial cells by inhibiting endothelial cell proliferation, survival and differentiation. It is unclear whether it has histone methyltransferase activity in vivo. According to some authors, it does not act as a histone methyltransferase by itself and represses transcription by recruiting EHMT2/G9a. According to others, it possesses histone methyltransferase activity when associated with other proteins and specifically methylates 'Lys-20' of histone H4 in vitro. 'Lys-20' methylation represents a specific tag for epigenetic transcriptional repression.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in histone-lysine N-methyltransferase activity
Specific function:
Not Available
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Coenzyme transport and metabolism
Specific function:
Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Gene Name:
Uniprot ID:
Molecular weight:
2-Hexaprenyl-6-methoxy-1,4-benzoquinone + S-Adenosylmethionine → 2-Hexaprenyl-3-methyl-6-methoxy-1,4 benzoquinone + S-Adenosylhomocysteinedetails
General function:
Involved in [myelin basic protein]-arginine N-methyltra
Specific function:
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Replication, recombination and repair
Specific function:
Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells. Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing. Promotes tumor growth.
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + Glycine → S-Adenosylhomocysteine + Sarcosinedetails
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Not Available
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine).
Gene Name:
Uniprot ID:
Molecular weight:
5-Hydroxyindoleacetic acid + S-Adenosylmethionine → 5-Methoxyindoleacetate + S-Adenosylhomocysteinedetails
N-Acetylserotonin + S-Adenosylmethionine → Melatonin + S-Adenosylhomocysteinedetails
General function:
Involved in histone-arginine N-methyltransferase activity
Specific function:
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H and may regulate its transcriptional elongation properties (By similarity). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (By similarity). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner. Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression. Symmetrically methylates NCL (By similarity). Methylates TP53; methylation might possibly affect TP53 target gene specificity (By similarity). Involved in spliceosome maturation and mRNA splicing in prophase I spermatocytes through the catalysis of the symmetrical arginine dimethylation of SNRPB (small nuclear ribonucleoprotein-associated protein B) and the interaction with tudor domain-containing protein TDRD6 (By similarity).
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in guanidinoacetate N-methyltransferase activity
Specific function:
Converts guanidinoacetate to creatine, using S-adenosylmethionine as the methyl donor. Important in nervous system development.
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + Guanidoacetic acid → S-Adenosylhomocysteine + Creatinedetails
Guanidoacetic acid + S-Adenosylhomocysteine → S-Adenosylmethionine + Creatinedetails
General function:
Coenzyme transport and metabolism
Specific function:
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + 3-Hexaprenyl-4,5-Dihydroxybenzoic acid → S-Adenosylhomocysteine + 3-Hexaprenyl-4-hydroxy-5-methoxybenzoic aciddetails
General function:
Involved in histone binding
Specific function:
Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates. Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a. H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3). Acts as a transcriptional repressor of various genes such as HOXA2, THBS1 and TP53 (By similarity). Repression of TP53 blocks cellular senescence (By similarity). Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (POLB), leading to the stimulation of its polymerase activity by enhancing DNA binding and processivity. Methylates HMGA1. Regulates alternative splicing events. Acts as a transcriptional coactivator of a number of steroid hormone receptors including ESR1, ESR2, PGR and NR3C1. Promotes fasting-induced transcriptional activation of the gluconeogenic program through methylation of the CRTC2 transcription coactivator. Methylates GPS2, protecting GPS2 from ubiquitination and degradation. Methylates SIRT7, inhibiting SIRT7 histone deacetylase activity and promoting mitochondria biogenesis (By similarity).
Gene Name:
Uniprot ID:
Molecular weight:
L-Histidine + S-Adenosylmethionine → 3-Methylhistidine + S-Adenosylhomocysteinedetails
General function:
Involved in chromatin binding
Specific function:
Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation (By similarity).
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in DNA binding
Specific function:
Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell derivation and self-renewal, suggesting that it is involved in safeguarding embryonic stem cell identity. Compared to EZH2-containing complexes, it is less abundant in embryonic stem cells, has weak methyltransferase activity and plays a less critical role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in histone-lysine N-methyltransferase activity
Specific function:
Histone methyltransferase that specifically methylates monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2) of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2) and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription and maintenance of genome integrity. In vitro also methylates unmodified 'Lys-20' (H4K20me0) of histone H4 and nucleosomes (By similarity). H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity). Plays a role in myogenesis by regulating the expression of target genes, such as EID3. Facilitates TP53BP1 foci formation upon DNA damage and proficient non-homologous end-joining (NHEJ)-directed DNA repair by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity). May play a role in class switch reconbination by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity).
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in phosphatidylethanolamine N-methyltransferas
Specific function:
Catalyzes the three sequential steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME), PMME to phosphatidyldimethylethanolamine (PDME), and PDME to phosphatidylcholine (PC).
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + Phosphatidyl-N-dimethylethanolamine → S-Adenosylhomocysteine + Phosphatidylcholinedetails
S-Adenosylmethionine + an L-1-Phosphatidylethanolamine → S-Adenosylhomocysteine + Phosphatidyl-N-methylethanolaminedetails
S-Adenosylmethionine + Phosphatidyl-N-methylethanolamine → S-Adenosylhomocysteine + Phosphatidyl-N-dimethylethanolaminedetails
S-Adenosylmethionine + PE(16:0/16:0) → S-Adenosylhomocysteine + PE-NMe(16:0/16:0)details
PE-NMe(16:0/16:0) + S-Adenosylmethionine → PE-NMe2(16:0/16:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(16:0/16:0) → S-Adenosylhomocysteine + PC(16:0/16:0)details
S-Adenosylmethionine + PE(16:0/18:0) → S-Adenosylhomocysteine + PE-NMe(16:0/18:0)details
PE-NMe(16:0/18:0) + S-Adenosylmethionine → PE-NMe2(16:0/18:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(16:0/18:0) → S-Adenosylhomocysteine + PC(16:0/18:0)details
S-Adenosylmethionine + PE(16:0/18:1(11Z)) → S-Adenosylhomocysteine + PE-NMe(16:0/18:1(11Z))details
PE-NMe(16:0/18:1(11Z)) + S-Adenosylmethionine → PE-NMe2(16:0/18:1(11Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(16:0/18:1(11Z)) → S-Adenosylhomocysteine + PC(16:0/18:1(11Z))details
S-Adenosylmethionine + PE(16:0/18:1(9Z)) → S-Adenosylhomocysteine + PE-NMe(16:0/18:1(9Z))details
PE-NMe(16:0/18:1(9Z)) + S-Adenosylmethionine → PE-NMe2(16:0/18:1(9Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(16:0/18:1(9Z)) → S-Adenosylhomocysteine + PC(16:0/18:1(9Z))details
S-Adenosylmethionine + PE(16:0/18:2(9Z,12Z)) → S-Adenosylhomocysteine + PE-NMe(16:0/18:2(9Z,12Z))details
PE-NMe(16:0/18:2(9Z,12Z)) + S-Adenosylmethionine → PE-NMe2(16:0/18:2(9Z,12Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(16:0/18:2(9Z,12Z)) → S-Adenosylhomocysteine + PC(16:0/18:2(9Z,12Z))details
S-Adenosylmethionine + PE(16:0/18:3(6Z,9Z,12Z)) → S-Adenosylhomocysteine + PE-NMe(16:0/18:3(6Z,9Z,12Z))details
PE-NMe(16:0/18:3(6Z,9Z,12Z)) + S-Adenosylmethionine → PE-NMe2(16:0/18:3(6Z,9Z,12Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(16:0/18:3(6Z,9Z,12Z)) → S-Adenosylhomocysteine + PC(16:0/18:3(6Z,9Z,12Z))details
S-Adenosylmethionine + PE(16:0/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PE-NMe(16:0/18:3(9Z,12Z,15Z))details
PE-NMe(16:0/18:3(9Z,12Z,15Z)) + S-Adenosylmethionine → PE-NMe2(16:0/18:3(9Z,12Z,15Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(16:0/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PC(16:0/18:3(9Z,12Z,15Z))details
S-Adenosylmethionine + PE(16:0/20:0) → S-Adenosylhomocysteine + PE-NMe(16:0/20:0)details
PE-NMe(16:0/20:0) + S-Adenosylmethionine → PE-NMe2(16:0/20:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(16:0/20:0) → S-Adenosylhomocysteine + PC(16:0/20:0)details
S-Adenosylmethionine + PE(16:0/20:1(11Z)) → S-Adenosylhomocysteine + PE-NMe(16:0/20:1(11Z))details
PE-NMe(16:0/20:1(11Z)) + S-Adenosylmethionine → PE-NMe2(16:0/20:1(11Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(16:0/20:1(11Z)) → S-Adenosylhomocysteine + PC(16:0/20:1(11Z))details
S-Adenosylmethionine + PE(16:0/22:0) → S-Adenosylhomocysteine + PE-NMe(16:0/22:0)details
PE-NMe(16:0/22:0) + S-Adenosylmethionine → PE-NMe2(16:0/22:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(16:0/22:0) → S-Adenosylhomocysteine + PC(16:0/22:0)details
S-Adenosylmethionine + PE(16:0/22:1(13Z)) → S-Adenosylhomocysteine + PE-NMe(16:0/22:1(13Z))details
PE-NMe(16:0/22:1(13Z)) + S-Adenosylmethionine → PE-NMe2(16:0/22:1(13Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(16:0/22:1(13Z)) → S-Adenosylhomocysteine + PC(16:0/22:1(13Z))details
S-Adenosylmethionine + PE(18:0/18:0) → S-Adenosylhomocysteine + PE-NMe(18:0/18:0)details
PE-NMe(18:0/18:0) + S-Adenosylmethionine → PE-NMe2(18:0/18:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:0/18:0) → S-Adenosylhomocysteine + PC(18:0/18:0)details
S-Adenosylmethionine + PE(18:0/18:1(11Z)) → S-Adenosylhomocysteine + PE-NMe(18:0/18:1(11Z))details
PE-NMe(18:0/18:1(11Z)) + S-Adenosylmethionine → PE-NMe2(18:0/18:1(11Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:0/18:1(11Z)) → S-Adenosylhomocysteine + PC(18:0/18:1(11Z))details
S-Adenosylmethionine + PE(18:0/18:1(9Z)) → S-Adenosylhomocysteine + PE-NMe(18:0/18:1(9Z))details
PE-NMe(18:0/18:1(9Z)) + S-Adenosylmethionine → PE-NMe2(18:0/18:1(9Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:0/18:1(9Z)) → S-Adenosylhomocysteine + PC(18:0/18:1(9Z))details
S-Adenosylmethionine + PE(18:0/18:2(9Z,12Z)) → S-Adenosylhomocysteine + PE-NMe(18:0/18:2(9Z,12Z))details
PE-NMe(18:0/18:2(9Z,12Z)) + S-Adenosylmethionine → PE-NMe2(18:0/18:2(9Z,12Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:0/18:2(9Z,12Z)) → S-Adenosylhomocysteine + PC(18:0/18:2(9Z,12Z))details
S-Adenosylmethionine + PE(18:0/18:3(6Z,9Z,12Z)) → S-Adenosylhomocysteine + PE-NMe(18:0/18:3(6Z,9Z,12Z))details
PE-NMe(18:0/18:3(6Z,9Z,12Z)) + S-Adenosylmethionine → PE-NMe2(18:0/18:3(6Z,9Z,12Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:0/18:3(6Z,9Z,12Z)) → S-Adenosylhomocysteine + PC(18:0/18:3(6Z,9Z,12Z))details
S-Adenosylmethionine + PE(18:0/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PE-NMe(18:0/18:3(9Z,12Z,15Z))details
PE-NMe(18:0/18:3(9Z,12Z,15Z)) + S-Adenosylmethionine → PE-NMe2(18:0/18:3(9Z,12Z,15Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:0/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PC(18:0/18:3(9Z,12Z,15Z))details
S-Adenosylmethionine + PE(18:0/20:0) → S-Adenosylhomocysteine + PE-NMe(18:0/20:0)details
PE-NMe(18:0/20:0) + S-Adenosylmethionine → PE-NMe2(18:0/20:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:0/20:0) → S-Adenosylhomocysteine + PC(18:0/20:0)details
S-Adenosylmethionine + PE(18:0/20:1(11Z)) → S-Adenosylhomocysteine + PE-NMe(18:0/20:1(11Z))details
PE-NMe(18:0/20:1(11Z)) + S-Adenosylmethionine → PE-NMe2(18:0/20:1(11Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:0/20:1(11Z)) → S-Adenosylhomocysteine + PC(18:0/20:1(11Z))details
S-Adenosylmethionine + PE(18:0/22:0) → S-Adenosylhomocysteine + PE-NMe(18:0/22:0)details
PE-NMe(18:0/22:0) + S-Adenosylmethionine → PE-NMe2(18:0/22:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:0/22:0) → S-Adenosylhomocysteine + PC(18:0/22:0)details
S-Adenosylmethionine + PE(18:0/22:1(13Z)) → S-Adenosylhomocysteine + PE-NMe(18:0/22:1(13Z))details
PE-NMe(18:0/22:1(13Z)) + S-Adenosylmethionine → PE-NMe2(18:0/22:1(13Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:0/22:1(13Z)) → S-Adenosylhomocysteine + PC(18:0/22:1(13Z))details
S-Adenosylmethionine + PE(18:1(11Z)/18:1(11Z)) → S-Adenosylhomocysteine + PE-NMe(18:1(11Z)/18:1(11Z))details
PE-NMe(18:1(11Z)/18:1(11Z)) + S-Adenosylmethionine → PE-NMe2(18:1(11Z)/18:1(11Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(11Z)/18:1(11Z)) → S-Adenosylhomocysteine + PC(18:1(11Z)/18:1(11Z))details
S-Adenosylmethionine + PE(18:1(11Z)/18:2(9Z,12Z)) → S-Adenosylhomocysteine + PE-NMe(18:1(11Z)/18:2(9Z,12Z))details
PE-NMe(18:1(11Z)/18:2(9Z,12Z)) + S-Adenosylmethionine → PE-NMe2(18:1(11Z)/18:2(9Z,12Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(11Z)/18:2(9Z,12Z)) → S-Adenosylhomocysteine + PC(18:1(11Z)/18:2(9Z,12Z))details
S-Adenosylmethionine + PE(18:1(11Z)/18:3(6Z,9Z,12Z)) → S-Adenosylhomocysteine + PE-NMe(18:1(11Z)/18:3(6Z,9Z,12Z))details
PE-NMe(18:1(11Z)/18:3(6Z,9Z,12Z)) + S-Adenosylmethionine → PE-NMe2(18:1(11Z)/18:3(6Z,9Z,12Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(11Z)/18:3(6Z,9Z,12Z)) → S-Adenosylhomocysteine + PC(18:1(11Z)/18:3(6Z,9Z,12Z))details
S-Adenosylmethionine + PE(18:1(11Z)/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PE-NMe(18:1(11Z)/18:3(9Z,12Z,15Z))details
PE-NMe(18:1(11Z)/18:3(9Z,12Z,15Z)) + S-Adenosylmethionine → PE-NMe2(18:1(11Z)/18:3(9Z,12Z,15Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(11Z)/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PC(18:1(11Z)/18:3(9Z,12Z,15Z))details
S-Adenosylmethionine + PE(18:1(11Z)/20:0) → S-Adenosylhomocysteine + PE-NMe(18:1(11Z)/20:0)details
PE-NMe(18:1(11Z)/20:0) + S-Adenosylmethionine → PE-NMe2(18:1(11Z)/20:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(11Z)/20:0) → S-Adenosylhomocysteine + PC(18:1(11Z)/20:0)details
S-Adenosylmethionine + PE(18:1(11Z)/20:1(11Z)) → S-Adenosylhomocysteine + PE-NMe(18:1(11Z)/20:1(11Z))details
PE-NMe(18:1(11Z)/20:1(11Z)) + S-Adenosylmethionine → PE-NMe2(18:1(11Z)/20:1(11Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(11Z)/20:1(11Z)) → S-Adenosylhomocysteine + PC(18:1(11Z)/20:1(11Z))details
S-Adenosylmethionine + PE(18:1(11Z)/22:0) → S-Adenosylhomocysteine + PE-NMe(18:1(11Z)/22:0)details
PE-NMe(18:1(11Z)/22:0) + S-Adenosylmethionine → PE-NMe2(18:1(11Z)/22:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(11Z)/22:0) → S-Adenosylhomocysteine + PC(18:1(11Z)/22:0)details
S-Adenosylmethionine + PE(18:1(11Z)/22:1(13Z)) → S-Adenosylhomocysteine + PE-NMe(18:1(11Z)/22:1(13Z))details
PE-NMe(18:1(11Z)/22:1(13Z)) + S-Adenosylmethionine → PE-NMe2(18:1(11Z)/22:1(13Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(11Z)/22:1(13Z)) → S-Adenosylhomocysteine + PC(18:1(11Z)/22:1(13Z))details
S-Adenosylmethionine + PE(18:1(9Z)/18:1(9Z)) → S-Adenosylhomocysteine + PE-NMe(18:1(9Z)/18:1(9Z))details
PE-NMe(18:1(9Z)/18:1(9Z)) + S-Adenosylmethionine → PE-NMe2(18:1(9Z)/18:1(9Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(9Z)/18:1(9Z)) → S-Adenosylhomocysteine + PC(18:1(9Z)/18:1(9Z))details
S-Adenosylmethionine + PE(18:1(9Z)/18:2(9Z,12Z)) → S-Adenosylhomocysteine + PE-NMe(18:1(9Z)/18:2(9Z,12Z))details
PE-NMe(18:1(9Z)/18:2(9Z,12Z)) + S-Adenosylmethionine → PE-NMe2(18:1(9Z)/18:2(9Z,12Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(9Z)/18:2(9Z,12Z)) → S-Adenosylhomocysteine + PC(18:1(9Z)/18:2(9Z,12Z))details
S-Adenosylmethionine + PE(18:1(9Z)/18:3(6Z,9Z,12Z)) → S-Adenosylhomocysteine + PE-NMe(18:1(9Z)/18:3(6Z,9Z,12Z))details
PE-NMe(18:1(9Z)/18:3(6Z,9Z,12Z)) + S-Adenosylmethionine → PE-NMe2(18:1(9Z)/18:3(6Z,9Z,12Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(9Z)/18:3(6Z,9Z,12Z)) → S-Adenosylhomocysteine + PC(18:1(9Z)/18:3(6Z,9Z,12Z))details
S-Adenosylmethionine + PE(18:1(9Z)/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PE-NMe(18:1(9Z)/18:3(9Z,12Z,15Z))details
PE-NMe(18:1(9Z)/18:3(9Z,12Z,15Z)) + S-Adenosylmethionine → PE-NMe2(18:1(9Z)/18:3(9Z,12Z,15Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(9Z)/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PC(18:1(9Z)/18:3(9Z,12Z,15Z))details
S-Adenosylmethionine + PE(18:1(9Z)/20:0) → S-Adenosylhomocysteine + PE-NMe(18:1(9Z)/20:0)details
PE-NMe(18:1(9Z)/20:0) + S-Adenosylmethionine → PE-NMe2(18:1(9Z)/20:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(9Z)/20:0) → S-Adenosylhomocysteine + PC(18:1(9Z)/20:0)details
S-Adenosylmethionine + PE(18:1(9Z)/20:1(11Z)) → S-Adenosylhomocysteine + PE-NMe(18:1(9Z)/20:1(11Z))details
PE-NMe(18:1(9Z)/20:1(11Z)) + S-Adenosylmethionine → PE-NMe2(18:1(9Z)/20:1(11Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(9Z)/20:1(11Z)) → S-Adenosylhomocysteine + PC(18:1(9Z)/20:1(11Z))details
S-Adenosylmethionine + PE(18:1(9Z)/22:0) → S-Adenosylhomocysteine + PE-NMe(18:1(9Z)/22:0)details
PE-NMe(18:1(9Z)/22:0) + S-Adenosylmethionine → PE-NMe2(18:1(9Z)/22:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(9Z)/22:0) → S-Adenosylhomocysteine + PC(18:1(9Z)/22:0)details
S-Adenosylmethionine + PE(18:1(9Z)/22:1(13Z)) → S-Adenosylhomocysteine + PE-NMe(18:1(9Z)/22:1(13Z))details
PE-NMe(18:1(9Z)/22:1(13Z)) + S-Adenosylmethionine → PE-NMe2(18:1(9Z)/22:1(13Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:1(9Z)/22:1(13Z)) → S-Adenosylhomocysteine + PC(18:1(9Z)/22:1(13Z))details
S-Adenosylmethionine + PE(18:2(9Z,12Z)/18:2(9Z,12Z)) → S-Adenosylhomocysteine + PE-NMe(18:2(9Z,12Z)/18:2(9Z,12Z))details
PE-NMe(18:2(9Z,12Z)/18:2(9Z,12Z)) + S-Adenosylmethionine → PE-NMe2(18:2(9Z,12Z)/18:2(9Z,12Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:2(9Z,12Z)/18:2(9Z,12Z)) → S-Adenosylhomocysteine + PC(18:2(9Z,12Z)/18:2(9Z,12Z))details
S-Adenosylmethionine + PE(18:2(9Z,12Z)/18:3(6Z,9Z,12Z)) → S-Adenosylhomocysteine + PE-NMe(18:2(9Z,12Z)/18:3(6Z,9Z,12Z))details
PE-NMe(18:2(9Z,12Z)/18:3(6Z,9Z,12Z)) + S-Adenosylmethionine → PE-NMe2(18:2(9Z,12Z)/18:3(6Z,9Z,12Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:2(9Z,12Z)/18:3(6Z,9Z,12Z)) → S-Adenosylhomocysteine + PC(18:2(9Z,12Z)/18:3(6Z,9Z,12Z))details
S-Adenosylmethionine + PE(18:2(9Z,12Z)/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PE-NMe(18:2(9Z,12Z)/18:3(9Z,12Z,15Z))details
PE-NMe(18:2(9Z,12Z)/18:3(9Z,12Z,15Z)) + S-Adenosylmethionine → PE-NMe2(18:2(9Z,12Z)/18:3(9Z,12Z,15Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:2(9Z,12Z)/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PC(18:2(9Z,12Z)/18:3(9Z,12Z,15Z))details
S-Adenosylmethionine + PE(18:2(9Z,12Z)/20:0) → S-Adenosylhomocysteine + PE-NMe(18:2(9Z,12Z)/20:0)details
PE-NMe(18:2(9Z,12Z)/20:0) + S-Adenosylmethionine → PE-NMe2(18:2(9Z,12Z)/20:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:2(9Z,12Z)/20:0) → S-Adenosylhomocysteine + PC(18:2(9Z,12Z)/20:0)details
S-Adenosylmethionine + PE(18:2(9Z,12Z)/20:1(11Z)) → S-Adenosylhomocysteine + PE-NMe(18:2(9Z,12Z)/20:1(11Z))details
PE-NMe(18:2(9Z,12Z)/20:1(11Z)) + S-Adenosylmethionine → PE-NMe2(18:2(9Z,12Z)/20:1(11Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:2(9Z,12Z)/20:1(11Z)) → S-Adenosylhomocysteine + PC(18:2(9Z,12Z)/20:1(11Z))details
S-Adenosylmethionine + PE(18:2(9Z,12Z)/22:0) → S-Adenosylhomocysteine + PE-NMe(18:2(9Z,12Z)/22:0)details
PE-NMe(18:2(9Z,12Z)/22:0) + S-Adenosylmethionine → PE-NMe2(18:2(9Z,12Z)/22:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:2(9Z,12Z)/22:0) → S-Adenosylhomocysteine + PC(18:2(9Z,12Z)/22:0)details
S-Adenosylmethionine + PE(18:2(9Z,12Z)/22:1(13Z)) → S-Adenosylhomocysteine + PE-NMe(18:2(9Z,12Z)/22:1(13Z))details
PE-NMe(18:2(9Z,12Z)/22:1(13Z)) + S-Adenosylmethionine → PE-NMe2(18:2(9Z,12Z)/22:1(13Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:2(9Z,12Z)/22:1(13Z)) → S-Adenosylhomocysteine + PC(18:2(9Z,12Z)/22:1(13Z))details
S-Adenosylmethionine + PE(18:3(6Z,9Z,12Z)/18:3(6Z,9Z,12Z)) → S-Adenosylhomocysteine + PE-NMe(18:3(6Z,9Z,12Z)/18:3(6Z,9Z,12Z))details
PE-NMe(18:3(6Z,9Z,12Z)/18:3(6Z,9Z,12Z)) + S-Adenosylmethionine → PE-NMe2(18:3(6Z,9Z,12Z)/18:3(6Z,9Z,12Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:3(6Z,9Z,12Z)/18:3(6Z,9Z,12Z)) → S-Adenosylhomocysteine + PC(18:3(6Z,9Z,12Z)/18:3(6Z,9Z,12Z))details
S-Adenosylmethionine + PE(18:3(6Z,9Z,12Z)/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PE-NMe(18:3(6Z,9Z,12Z)/18:3(9Z,12Z,15Z))details
PE-NMe(18:3(6Z,9Z,12Z)/18:3(9Z,12Z,15Z)) + S-Adenosylmethionine → PE-NMe2(18:3(6Z,9Z,12Z)/18:3(9Z,12Z,15Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:3(6Z,9Z,12Z)/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PC(18:3(6Z,9Z,12Z)/18:3(9Z,12Z,15Z))details
S-Adenosylmethionine + PE(18:3(6Z,9Z,12Z)/20:0) → S-Adenosylhomocysteine + PE-NMe(18:3(6Z,9Z,12Z)/20:0)details
PE-NMe(18:3(6Z,9Z,12Z)/20:0) + S-Adenosylmethionine → PE-NMe2(18:3(6Z,9Z,12Z)/20:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:3(6Z,9Z,12Z)/20:0) → S-Adenosylhomocysteine + PC(18:3(6Z,9Z,12Z)/20:0)details
S-Adenosylmethionine + PE(18:3(6Z,9Z,12Z)/20:1(11Z)) → S-Adenosylhomocysteine + PE-NMe(18:3(6Z,9Z,12Z)/20:1(11Z))details
PE-NMe(18:3(6Z,9Z,12Z)/20:1(11Z)) + S-Adenosylmethionine → PE-NMe2(18:3(6Z,9Z,12Z)/20:1(11Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:3(6Z,9Z,12Z)/20:1(11Z)) → S-Adenosylhomocysteine + PC(18:3(6Z,9Z,12Z)/20:1(11Z))details
S-Adenosylmethionine + PE(18:3(6Z,9Z,12Z)/22:0) → S-Adenosylhomocysteine + PE-NMe(18:3(6Z,9Z,12Z)/22:0)details
PE-NMe(18:3(6Z,9Z,12Z)/22:0) + S-Adenosylmethionine → PE-NMe2(18:3(6Z,9Z,12Z)/22:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:3(6Z,9Z,12Z)/22:0) → S-Adenosylhomocysteine + PC(18:3(6Z,9Z,12Z)/22:0)details
S-Adenosylmethionine + PE(18:3(6Z,9Z,12Z)/22:1(13Z)) → S-Adenosylhomocysteine + PE-NMe(18:3(6Z,9Z,12Z)/22:1(13Z))details
PE-NMe(18:3(6Z,9Z,12Z)/22:1(13Z)) + S-Adenosylmethionine → PE-NMe2(18:3(6Z,9Z,12Z)/22:1(13Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:3(6Z,9Z,12Z)/22:1(13Z)) → S-Adenosylhomocysteine + PC(18:3(6Z,9Z,12Z)/22:1(13Z))details
S-Adenosylmethionine + PE(18:3(9Z,12Z,15Z)/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PE-NMe(18:3(9Z,12Z,15Z)/18:3(9Z,12Z,15Z))details
PE-NMe(18:3(9Z,12Z,15Z)/18:3(9Z,12Z,15Z)) + S-Adenosylmethionine → PE-NMe2(18:3(9Z,12Z,15Z)/18:3(9Z,12Z,15Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:3(9Z,12Z,15Z)/18:3(9Z,12Z,15Z)) → S-Adenosylhomocysteine + PC(18:3(9Z,12Z,15Z)/18:3(9Z,12Z,15Z))details
S-Adenosylmethionine + PE(18:3(9Z,12Z,15Z)/20:0) → S-Adenosylhomocysteine + PE-NMe(18:3(9Z,12Z,15Z)/20:0)details
PE-NMe(18:3(9Z,12Z,15Z)/20:0) + S-Adenosylmethionine → PE-NMe2(18:3(9Z,12Z,15Z)/20:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:3(9Z,12Z,15Z)/20:0) → S-Adenosylhomocysteine + PC(18:3(9Z,12Z,15Z)/20:0)details
S-Adenosylmethionine + PE(18:3(9Z,12Z,15Z)/20:1(11Z)) → S-Adenosylhomocysteine + PE-NMe(18:3(9Z,12Z,15Z)/20:1(11Z))details
PE-NMe(18:3(9Z,12Z,15Z)/20:1(11Z)) + S-Adenosylmethionine → PE-NMe2(18:3(9Z,12Z,15Z)/20:1(11Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:3(9Z,12Z,15Z)/20:1(11Z)) → S-Adenosylhomocysteine + PC(18:3(9Z,12Z,15Z)/20:1(11Z))details
S-Adenosylmethionine + PE(18:3(9Z,12Z,15Z)/22:0) → S-Adenosylhomocysteine + PE-NMe(18:3(9Z,12Z,15Z)/22:0)details
PE-NMe(18:3(9Z,12Z,15Z)/22:0) + S-Adenosylmethionine → PE-NMe2(18:3(9Z,12Z,15Z)/22:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:3(9Z,12Z,15Z)/22:0) → S-Adenosylhomocysteine + PC(18:3(9Z,12Z,15Z)/22:0)details
S-Adenosylmethionine + PE(18:3(9Z,12Z,15Z)/22:1(13Z)) → S-Adenosylhomocysteine + PE-NMe(18:3(9Z,12Z,15Z)/22:1(13Z))details
PE-NMe(18:3(9Z,12Z,15Z)/22:1(13Z)) + S-Adenosylmethionine → PE-NMe2(18:3(9Z,12Z,15Z)/22:1(13Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(18:3(9Z,12Z,15Z)/22:1(13Z)) → S-Adenosylhomocysteine + PC(18:3(9Z,12Z,15Z)/22:1(13Z))details
S-Adenosylmethionine + PE(20:0/20:0) → S-Adenosylhomocysteine + PE-NMe(20:0/20:0)details
PE-NMe(20:0/20:0) + S-Adenosylmethionine → PE-NMe2(20:0/20:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(20:0/20:0) → S-Adenosylhomocysteine + PC(20:0/20:0)details
S-Adenosylmethionine + PE(20:0/20:1(11Z)) → S-Adenosylhomocysteine + PE-NMe(20:0/20:1(11Z))details
PE-NMe(20:0/20:1(11Z)) + S-Adenosylmethionine → PE-NMe2(20:0/20:1(11Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(20:0/20:1(11Z)) → S-Adenosylhomocysteine + PC(20:0/20:1(11Z))details
S-Adenosylmethionine + PE(20:0/22:0) → S-Adenosylhomocysteine + PE-NMe(20:0/22:0)details
PE-NMe(20:0/22:0) + S-Adenosylmethionine → PE-NMe2(20:0/22:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(20:0/22:0) → S-Adenosylhomocysteine + PC(20:0/22:0)details
S-Adenosylmethionine + PE(20:0/22:1(13Z)) → S-Adenosylhomocysteine + PE-NMe(20:0/22:1(13Z))details
PE-NMe(20:0/22:1(13Z)) + S-Adenosylmethionine → PE-NMe2(20:0/22:1(13Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(20:0/22:1(13Z)) → S-Adenosylhomocysteine + PC(20:0/22:1(13Z))details
S-Adenosylmethionine + PE(20:1(11Z)/20:1(11Z)) → S-Adenosylhomocysteine + PE-NMe(20:1(11Z)/20:1(11Z))details
PE-NMe(20:1(11Z)/20:1(11Z)) + S-Adenosylmethionine → PE-NMe2(20:1(11Z)/20:1(11Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(20:1(11Z)/20:1(11Z)) → S-Adenosylhomocysteine + PC(20:1(11Z)/20:1(11Z))details
S-Adenosylmethionine + PE(20:1(11Z)/22:0) → S-Adenosylhomocysteine + PE-NMe(20:1(11Z)/22:0)details
PE-NMe(20:1(11Z)/22:0) + S-Adenosylmethionine → PE-NMe2(20:1(11Z)/22:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(20:1(11Z)/22:0) → S-Adenosylhomocysteine + PC(20:1(11Z)/22:0)details
S-Adenosylmethionine + PE(20:1(11Z)/22:1(13Z)) → S-Adenosylhomocysteine + PE-NMe(20:1(11Z)/22:1(13Z))details
PE-NMe(20:1(11Z)/22:1(13Z)) + S-Adenosylmethionine → PE-NMe2(20:1(11Z)/22:1(13Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(20:1(11Z)/22:1(13Z)) → S-Adenosylhomocysteine + PC(20:1(11Z)/22:1(13Z))details
S-Adenosylmethionine + PE(22:0/22:0) → S-Adenosylhomocysteine + PE-NMe(22:0/22:0)details
PE-NMe(22:0/22:0) + S-Adenosylmethionine → PE-NMe2(22:0/22:0) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(22:0/22:0) → S-Adenosylhomocysteine + PC(22:0/22:0)details
S-Adenosylmethionine + PE(22:0/22:1(13Z)) → S-Adenosylhomocysteine + PE-NMe(22:0/22:1(13Z))details
PE-NMe(22:0/22:1(13Z)) + S-Adenosylmethionine → PE-NMe2(22:0/22:1(13Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(22:0/22:1(13Z)) → S-Adenosylhomocysteine + PC(22:0/22:1(13Z))details
S-Adenosylmethionine + PE(22:1(13Z)/22:1(13Z)) → S-Adenosylhomocysteine + PE-NMe(22:1(13Z)/22:1(13Z))details
PE-NMe(22:1(13Z)/22:1(13Z)) + S-Adenosylmethionine → PE-NMe2(22:1(13Z)/22:1(13Z)) + S-Adenosylhomocysteinedetails
S-Adenosylmethionine + PE-NMe2(22:1(13Z)/22:1(13Z)) → S-Adenosylhomocysteine + PC(22:1(13Z)/22:1(13Z))details
General function:
Involved in catechol O-methyltransferase activity
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 (By similarity).
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + 2-Hydroxyestrone → 2-Methoxyestrone + S-Adenosylhomocysteinedetails
General function:
Involved in histone-lysine N-methyltransferase activity
Specific function:
Histone methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3, 2 specific tags for epigenetic transcriptional activation. Specifically mediates dimethylation of H3 'Lys-36'.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Coenzyme transport and metabolism
Specific function:
Not Available
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Coenzyme transport and metabolism
Specific function:
May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate (By similarity).
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Coenzyme transport and metabolism
Specific function:
Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylhomocysteine + Water → Homocysteine + Adenosinedetails
General function:
Not Available
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.
Gene Name:
Uniprot ID:
Molecular weight:
S-Adenosylmethionine + L-Lysine → S-Adenosylhomocysteine + N6,N6,N6-Trimethyl-L-lysinedetails