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Record Information
Version1.0
Creation Date2016-09-30 22:42:14 UTC
Update Date2020-05-21 16:28:30 UTC
BMDB IDBMDB0001185
Secondary Accession Numbers
  • BMDB01185
Metabolite Identification
Common NameS-Adenosylmethionine
DescriptionS-Adenosylmethionine, also known as SAM or adomet, 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-Adenosylmethionine is a very strong basic compound (based on its pKa). S-Adenosylmethionine exists in all living species, ranging from bacteria to humans. S-Adenosylmethionine is a potentially toxic compound.
Structure
Thumb
Synonyms
ValueSource
(3S)-5'-[(3-Amino-3-carboxypropyl)methylsulfonio]-5'-deoxyadenosine, inner saltChEBI
[1-(Adenin-9-yl)-1,5-dideoxy-beta-D-ribofuranos-5-yl][(3S)-3-amino-3-carboxypropyl](methyl)sulfoniumChEBI
AcylcarnitineChEBI
AdoMetChEBI
S-(5'-Deoxyadenosin-5'-yl)-L-methionineChEBI
SAMChEBI
SAMeChEBI
(3S)-5'-[(3-Amino-3-carboxypropyl)methylsulphonio]-5'-deoxyadenosine, inner saltGenerator
[1-(Adenin-9-yl)-1,5-dideoxy-b-D-ribofuranos-5-yl][(3S)-3-amino-3-carboxypropyl](methyl)sulfoniumGenerator
[1-(Adenin-9-yl)-1,5-dideoxy-b-D-ribofuranos-5-yl][(3S)-3-amino-3-carboxypropyl](methyl)sulphoniumGenerator
[1-(Adenin-9-yl)-1,5-dideoxy-beta-D-ribofuranos-5-yl][(3S)-3-amino-3-carboxypropyl](methyl)sulphoniumGenerator
[1-(Adenin-9-yl)-1,5-dideoxy-β-D-ribofuranos-5-yl][(3S)-3-amino-3-carboxypropyl](methyl)sulfoniumGenerator
[1-(Adenin-9-yl)-1,5-dideoxy-β-D-ribofuranos-5-yl][(3S)-3-amino-3-carboxypropyl](methyl)sulphoniumGenerator
(3S)-5'-[(3-Amino-3-carboxypropyl)methylsulfonio]-5'-deoxyadenosineHMDB
2-S-Adenosyl-L-methionineHMDB
5'-Deoxyadenosine-5'-L-methionine disulfate ditosylateHMDB
5'-Deoxyadenosine-5'-L-methionine disulphate ditosylateHMDB
Active methionineHMDB
AdemetionineHMDB
AdenosylmethionineHMDB
DonametHMDB
L-S-AdenosylmethionineHMDB
S-(5'-Adenosyl)-L-methionineHMDB
S-Adenosyl methionineHMDB
S-Adenosyl-L-methionineHMDB
S-Adenosyl-L-methionine disulfate tosylateHMDB
S-Adenosyl-L-methionine disulphate tosylateHMDB
S-Adenosyl-methionineHMDB
ASTA medica brand OF ademetionine tosilate disulfateHMDB
S Adenosylmethionine sulfate tosylateHMDB
S-Adenosylmethionine sulfate tosylateHMDB
Sulfate tosylate, S-adenosylmethionineHMDB
Ademetionine europharma brandHMDB
Amet, SHMDB
Europharma brand OF ademetionineHMDB
GumbaralHMDB
Knoll brand OF brand OF ademetionine tosilate disulfateHMDB
S AdenosylmethionineHMDB
S AmetHMDB
SamyrHMDB
Tosylate, S-adenosylmethionine sulfateHMDB
S Adenosyl L methionineHMDB
SAM-eHMDB
Chemical FormulaC15H23N6O5S
Average Molecular Weight399.445
Monoisotopic Molecular Weight399.145063566
IUPAC Name[(3S)-3-amino-3-carboxypropyl]({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl})methylsulfanium
Traditional NameSAMe
CAS Registry Number29908-03-0
SMILES
C[S+](CC[C@H](N)C(O)=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC2=C1N=CN=C2N
InChI Identifier
InChI=1S/C15H22N6O5S/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25)/p+1/t7-,8+,10+,11+,14+,27?/m0/s1
InChI KeyMEFKEPWMEQBLKI-AIRLBKTGSA-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
  • Methionine or derivatives
  • N-glycosyl compound
  • Glycosyl compound
  • Pentose monosaccharide
  • 6-aminopurine
  • Alpha-amino acid
  • L-alpha-amino acid
  • Alpha-amino acid or derivatives
  • Imidazopyrimidine
  • Purine
  • Aminopyrimidine
  • Hydroxy fatty acid
  • Thia fatty acid
  • N-substituted imidazole
  • Fatty acyl
  • Monosaccharide
  • Imidolactam
  • Pyrimidine
  • Azole
  • Imidazole
  • Heteroaromatic compound
  • Tetrahydrofuran
  • Amino acid or derivatives
  • 1,2-diol
  • Amino acid
  • Secondary alcohol
  • Oxacycle
  • Azacycle
  • Carboxylic acid derivative
  • Carboxylic acid
  • Organoheterocyclic compound
  • Monocarboxylic acid or derivatives
  • Organic oxide
  • Organopnictogen compound
  • Alcohol
  • Carbonyl group
  • Organic oxygen compound
  • Organic nitrogen compound
  • Hydrocarbon derivative
  • Primary amine
  • Organosulfur compound
  • Organooxygen compound
  • Primary aliphatic amine
  • Amine
  • Organonitrogen compound
  • Organic cation
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Ontology
StatusExpected but not Quantified
Origin
  • Endogenous
BiofunctionNot Available
ApplicationNot Available
Cellular locations
  • Cytoplasm
  • Endoplasmic reticulum
  • Mitochondria
  • Myelin sheath
  • Nucleus
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
logP-2ALOGPS
logP-5.3ChemAxon
logS-2.6ALOGPS
pKa (Strongest Acidic)1.7ChemAxon
pKa (Strongest Basic)9.41ChemAxon
Physiological Charge1ChemAxon
Hydrogen Acceptor Count10ChemAxon
Hydrogen Donor Count5ChemAxon
Polar Surface Area182.63 ŲChemAxon
Rotatable Bond Count7ChemAxon
Refractivity96.23 m³·mol⁻¹ChemAxon
Polarizability40.37 ųChemAxon
Number of Rings3ChemAxon
BioavailabilityYesChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash Key
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0a5c-5965000000-324e4a3cbf936132bcf1View in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (3 TMS) - 70eV, Positivesplash10-00ea-7958582000-3dd40cf273f182ee53ddView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-0002-0019000000-6dfa0dc65a9863755c2aView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-0udj-0293000000-57cc9d4430592060d41dView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-0udr-1940000000-ed4985bea80649d27efeView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-000b-8920000000-8f05e9898f0d26ddf3f8View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-000e-9400000000-e5c5617045d9915e8e46View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-IT , positivesplash10-0udi-0090000000-93017671648813ece8a5View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000i-0914000000-95030ceaf1c187dcf656View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-0900000000-c3fae8b7a68475b614a4View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-2900000000-44078fd7eaeafcc5bba8View in MoNA
Biological Properties
Cellular Locations
  • Cytoplasm
  • Endoplasmic reticulum
  • Mitochondria
  • Myelin sheath
  • Nucleus
Biospecimen Locations
  • Epidermis
  • Eye Lens
  • Fibroblasts
  • Intestine
  • Kidney
  • Neuron
  • Ovary
  • Placenta
  • Prostate Tissue
  • Skeletal Muscle
  • Testis
Pathways
Normal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
EpidermisExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
Eye LensExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
FibroblastsExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
IntestineExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
KidneyExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
NeuronExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
OvaryExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
PlacentaExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
Prostate TissueExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
Skeletal MuscleExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
TestisExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
Abnormal Concentrations
Not Available
HMDB IDHMDB0001185
DrugBank IDNot Available
Phenol Explorer Compound IDNot Available
FooDB IDFDB031152
KNApSAcK IDC00007347
Chemspider ID21169292
KEGG Compound IDC00019
BioCyc IDS-ADENOSYLMETHIONINE
BiGG ID33530
Wikipedia LinkS-Adenosyl_methionine
METLIN ID6064
PubChem Compound34756
PDB IDNot Available
ChEBI ID15414
References
Synthesis ReferenceLin, Jian-Ping; Tian, Jun; You, Jian-Feng; Jin, Zhi-Hua; Xu, Zhi-Nan; Cen, Pei-Lin. An effective strategy for the co-production of S-adenosyl-L-methionine and glutathione by fed-batch fermentation. Biochemical Engineering Journal (2004), 21(1), 19-25.
Material Safety Data Sheet (MSDS)Not Available
General ReferencesNot Available

Enzymes

General function:
Involved in phenylethanolamine N-methyltransferase acti
Specific function:
Converts noradrenaline to adrenaline.
Gene Name:
PNMT
Uniprot ID:
P10938
Molecular weight:
30918.0
Reactions
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:
HNMT
Uniprot ID:
Q58DV7
Molecular weight:
33646.0
Reactions
S-Adenosylmethionine + Histamine → S-Adenosylhomocysteine + 1-Methylhistaminedetails
General function:
Coenzyme transport and metabolism
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Gene Name:
MAT2A
Uniprot ID:
A7E3T7
Molecular weight:
43691.0
General function:
Transcription
Specific function:
Catalytic tRNA acetyltransferase subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). May also act as a protein lysine acetyltransferase by mediating acetylation of target proteins; such activity is however unclear in vivo and recent evidences suggest that ELP3 primarily acts as a tRNA acetyltransferase. Involved in neurogenesis: regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (By similarity). Required for acetylation of GJA1 in the developing cerebral cortex (By similarity).
Gene Name:
ELP3
Uniprot ID:
Q2KJ61
Molecular weight:
62331.0
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. Catalytic subunit of mRNA N(1)-methyltransferase complex, which mediates methylation of adenosine residues at the N(1) position of a small subset of mRNAs: N(1) methylation takes place in tRNA T-loop-like structures of mRNAs and is only present at low stoichiometries.
Gene Name:
TRMT61A
Uniprot ID:
A6H791
Molecular weight:
31047.0
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:
SUV39H2
Uniprot ID:
Q32PH7
Molecular weight:
46551.0
General function:
Coenzyme transport and metabolism
Specific function:
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Gene Name:
LIAS
Uniprot ID:
Q5BIP7
Molecular weight:
42035.0
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:
PCMT1
Uniprot ID:
P15246
Molecular weight:
24565.0
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:
KMT5A
Uniprot ID:
Q2YDJ8
Molecular weight:
39277.0
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:
DPH5
Uniprot ID:
Q5E982
Molecular weight:
31662.0
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:
PRDM6
Uniprot ID:
A6QPM3
Molecular weight:
63989.0
General function:
Replication, recombination and repair
Specific function:
Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp).
Gene Name:
TRDMT1
Uniprot ID:
Q7YS61
Molecular weight:
44570.0
General function:
Involved in histone-lysine N-methyltransferase activity
Specific function:
Not Available
Gene Name:
EHMT1
Uniprot ID:
A5PK11
Molecular weight:
138734.0
General function:
Coenzyme transport and metabolism
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Gene Name:
MAT1A
Uniprot ID:
Q2KJC6
Molecular weight:
43761.0
Reactions
Adenosine triphosphate + L-Methionine + Water → S-Adenosylmethionine + Hydrogen phosphate + Pyrophosphatedetails
General function:
Involved in tRNA (guanine-N1-)-methyltransferase activity
Specific function:
Involved in mitochondrial tRNA methylation (By similarity). Specifically methylates the N1 position of guanosine-37 in various tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.
Gene Name:
TRMT5
Uniprot ID:
Q3MHN8
Molecular weight:
56954.0
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:
COQ5
Uniprot ID:
Q0P5A2
Molecular weight:
37591.0
Reactions
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:
PRMT7
Uniprot ID:
A6QQV6
Molecular weight:
78654.0
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:
DNMT1
Uniprot ID:
Q24K09
Molecular weight:
182842.0
Reactions
S-Adenosylmethionine + Glycine → S-Adenosylhomocysteine + Sarcosinedetails
General function:
Replication, recombination and repair
Specific function:
Not Available
Gene Name:
Dnmt1
Uniprot ID:
B1P383
Molecular weight:
153086.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Not Available
Gene Name:
TPMT
Uniprot ID:
Q17QQ2
Molecular weight:
28335.0
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:
ASMT
Uniprot ID:
P10950
Molecular weight:
37924.0
Reactions
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:
PRMT5
Uniprot ID:
A7YW45
Molecular weight:
72629.0
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:
GAMT
Uniprot ID:
Q2TBQ3
Molecular weight:
26610.0
Reactions
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:
COQ3
Uniprot ID:
Q3T131
Molecular weight:
41490.0
Reactions
S-Adenosylmethionine + 3-Hexaprenyl-4,5-Dihydroxybenzoic acid → S-Adenosylhomocysteine + 3-Hexaprenyl-4-hydroxy-5-methoxybenzoic aciddetails
General function:
Amino acid transport and metabolism
Specific function:
Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity).
Gene Name:
MTR
Uniprot ID:
Q4JIJ3
Molecular weight:
140478.0
General function:
Involved in adenosylmethionine decarboxylase activity
Specific function:
Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels.
Gene Name:
AMD1
Uniprot ID:
P50243
Molecular weight:
38365.0
Reactions
S-Adenosylmethionine → S-Adenosylmethioninamine + Carbon dioxidedetails
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:
PRMT6
Uniprot ID:
Q5E9L5
Molecular weight:
41868.0
Reactions
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:
SUV39H1
Uniprot ID:
Q2NL30
Molecular weight:
47846.0
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:
EZH1
Uniprot ID:
A7E2Z2
Molecular weight:
85285.0
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:
KMT5B
Uniprot ID:
Q29RP8
Molecular weight:
44552.0
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:
PEMT
Uniprot ID:
Q7YRH6
Molecular weight:
22018.0
Reactions
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:
COMT
Uniprot ID:
A7MBI7
Molecular weight:
30485.0
Reactions
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:
SETMAR
Uniprot ID:
Q0VD24
Molecular weight:
34254.0
General function:
Involved in tRNA (guanine-N7-)-methyltransferase activity
Specific function:
Methyltransferase that mediates the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs). Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. Also acts as a methyltransferase for a subset of internal N(7)-methylguanine in mRNAs. Internal N(7)-methylguanine methylation of mRNAs regulates translation. Also methylates a specific subset of miRNAs, such as let-7. N(7)-methylguanine methylation of let-7 miRNA promotes let-7 miRNA processing by disrupting an inhibitory secondary structure within the primary miRNA transcript (pri-miRNA). Acts as a regulator of embryonic stem cell self-renewal and differentiation.
Gene Name:
METTL1
Uniprot ID:
Q2YDF1
Molecular weight:
31323.0
General function:
Coenzyme transport and metabolism
Specific function:
Interferon-inducible iron-sulfur (4FE-4S) cluster-binding antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Can inhibit a wide range of viruses, including west Nile virus (WNV), dengue virus, sindbis virus, influenza A virus, sendai virus and vesicular stomatitis virus (VSV). Displays antiviral activity against influenza A virus by inhibiting the budding of the virus from the plasma membrane by disturbing the lipid rafts. This is accomplished, at least in part, through binding and inhibition of the enzyme farnesyl diphosphate synthase (FPPS), which is essential for the biosynthesis of isoprenoid-derived lipids. Promotes TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating Lys-63'-linked ubiquitination of IRAK1. Plays a role in CD4+ T-cell activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins (By similarity).
Gene Name:
RSAD2
Uniprot ID:
Q2HJF9
Molecular weight:
41672.0
General function:
Coenzyme transport and metabolism
Specific function:
Isoform MOCS1A and isoform MOCS1B probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP). MOCS1A catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate and MOCS1B catalyzes the subsequent conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cPMP.
Gene Name:
MOCS1
Uniprot ID:
Q1JQD7
Molecular weight:
69659.0
General function:
Coenzyme transport and metabolism
Specific function:
May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen-III oxidase activity (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Gene Name:
RSAD1
Uniprot ID:
A5D7B1
Molecular weight:
48722.0
General function:
Involved in binding
Specific function:
Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Specifically mediates the transport of S-adenosylmethionine (SAM) into the mitochondria (By similarity).
Gene Name:
SLC25A26
Uniprot ID:
A6QR09
Molecular weight:
29409.0
General function:
Not Available
Specific function:
Regulatory subunit of S-adenosylmethionine synthetase 2, an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates MAT2A catalytic activity by changing its kinetic properties, increasing its affinity for L-methionine. Can bind NADP (in vitro).
Gene Name:
MAT2B
Uniprot ID:
Q29RI9
Molecular weight:
37768.0
Reactions
Adenosine triphosphate + L-Methionine + Water → S-Adenosylmethionine + Hydrogen phosphate + Pyrophosphatedetails
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:
SETD7
Uniprot ID:
F1MUT0
Molecular weight:
40648.0
Reactions
S-Adenosylmethionine + L-Lysine → S-Adenosylhomocysteine + N6,N6,N6-Trimethyl-L-lysinedetails