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Identification
YMDB IDYMDB00438
NameS-Adenosyl-L-methionine
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionS-Adenosyl-L-methionine (SAM) is a common co-substrate involved in methyl group transfers. It is made from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase [EC 2.5.1.6]. SAM is involved in transmethylation, transsulfuration, and aminopropylation metabolic pathways.
Structure
Thumb
Synonyms
  • (3S)-5'-[(3-amino-3-carboxypropyl)methylsulfonio]-5'-deoxyadenosine, inner salt
  • [1-(adenin-9-yl)-1,5-dideoxy-beta-D-ribofuranos-5-yl][(3S)-3-amino-3-carboxypropyl](methyl)sulfonium
  • 2-S-adenosyl-L-methionine
  • 5'-Deoxyadenosine-5'-L-methionine disulfate ditosylate
  • acylcarnitine
  • Ademetionine
  • adenosylmethionine
  • AdoMet
  • Donamet
  • L-S-Adenosylmethionine
  • S-(5'-Adenosyl)-L-methionine
  • S-(5'-deoxyadenosin-5'-yl)-L-methionine
  • S-adenosyl methionine
  • S-adenosyl-L-methionine
  • S-Adenosyl-L-Methionine Disulfate Tosylate
  • S-adenosyl-methionine
  • s-adenosylmethionine
  • SAM
  • SAM-e
  • SAMe
  • (3S)-5'-[(3-Amino-3-carboxypropyl)methylsulphonio]-5'-deoxyadenosine, inner salt
  • [1-(Adenin-9-yl)-1,5-dideoxy-b-D-ribofuranos-5-yl][(3S)-3-amino-3-carboxypropyl](methyl)sulfonium
  • [1-(Adenin-9-yl)-1,5-dideoxy-b-D-ribofuranos-5-yl][(3S)-3-amino-3-carboxypropyl](methyl)sulphonium
  • [1-(Adenin-9-yl)-1,5-dideoxy-beta-D-ribofuranos-5-yl][(3S)-3-amino-3-carboxypropyl](methyl)sulphonium
  • [1-(Adenin-9-yl)-1,5-dideoxy-β-D-ribofuranos-5-yl][(3S)-3-amino-3-carboxypropyl](methyl)sulfonium
  • [1-(Adenin-9-yl)-1,5-dideoxy-β-D-ribofuranos-5-yl][(3S)-3-amino-3-carboxypropyl](methyl)sulphonium
  • (3S)-5'-[(3-Amino-3-carboxypropyl)methylsulfonio]-5'-deoxyadenosine
  • 5'-Deoxyadenosine-5'-L-methionine disulphate ditosylate
  • Active methionine
  • S-Adenosyl-L-methionine disulphate tosylate
  • ASTA medica brand OF ademetionine tosilate disulfate
  • S Adenosylmethionine sulfate tosylate
  • S-Adenosylmethionine sulfate tosylate
  • Sulfate tosylate, S-adenosylmethionine
  • Ademetionine europharma brand
  • Amet, S
  • Europharma brand OF ademetionine
  • Gumbaral
  • Knoll brand OF brand OF ademetionine tosilate disulfate
  • S Adenosylmethionine
  • S Amet
  • Samyr
  • Tosylate, S-adenosylmethionine sulfate
  • S Adenosyl L methionine
CAS number29908-03-0
WeightAverage: 399.445
Monoisotopic: 399.145063566
InChI KeyMEFKEPWMEQBLKI-AIRLBKTGSA-O
InChIInChI=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
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 IUPAC NameSAMe
Chemical FormulaC15H23N6O5S
SMILESC[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
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
Physical Properties
StateSolid
Charge1
Melting pointNot Available
Experimental Properties
PropertyValueReference
Water SolubilityNot AvailablePhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility1.19 g/LALOGPS
logP-2ALOGPS
logP-5.3ChemAxon
logS-2.6ALOGPS
pKa (Strongest Acidic)1.71ChemAxon
pKa (Strongest Basic)9.41ChemAxon
Physiological Charge1ChemAxon
Hydrogen Acceptor Count10ChemAxon
Hydrogen Donor Count5ChemAxon
Polar Surface Area182.63 ŲChemAxon
Rotatable Bond Count7ChemAxon
Refractivity96.23 m³·mol⁻¹ChemAxon
Polarizability40.37 ųChemAxon
Number of Rings3ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • Cytoplasm, Endoplasmic Reticulum, Extracellular, Mitochondrion
Organoleptic PropertiesNot Available
SMPDB Pathways
Biotin BiosynthesisPW002380 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(10:0)PW002545 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(12:0)PW002548 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(14:0)PW002544 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(16:0)PW002550 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Arginine and proline metabolismec00330 Map00330
Cysteine and methionine metabolismec00270 Map00270
Lipoic acid metabolismec00785 Map00785
Steroid biosynthesisec00100 Map00100
beta-Alanine metabolismec00410 Map00410
SMPDB Reactions
8-Amino-7-oxononanoic acid + S-Adenosyl-L-methionineDiaminopimelic acid + S-adenosyl-4-methylthio-2-oxobutanoate
Dethiobiotin + S-Adenosyl-L-methionine + Reduced ferredoxin + a sulfurated [sulfur carrier]  → Biotin + L-Methionine + 5'-Deoxyadenosine + an unsulfurated [sulfur carrier] + Oxidized ferredoxin
S-Adenosyl-L-methionine + hydronS-Adenosylmethioninamine + Carbon dioxide
L-Methionine + Adenosine triphosphate + waterphosphate + Pyrophosphate + S-Adenosyl-L-methionine
S-Adenosyl-L-methionine + 3-Hexaprenyl-4,5-dihydroxybenzoic acidS-Adenosylhomocysteine + 3-Hexaprenyl-4-hydroxy-5-methoxybenzoic acid
KEGG ReactionsNot Available
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
References
References:
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Pirkov, I., Norbeck, J., Gustafsson, L., Albers, E. (2008). "A complete inventory of all enzymes in the eukaryotic methionine salvage pathway." FEBS J 275:4111-4120.18625006
  • Chiang, P. K., Cantoni, G. L. (1977). "Activation of methionine for transmethylation. Purification of the S-adenosylmethionine synthetase of bakers' yeast and its separation into two forms." J Biol Chem 252:4506-4513.194884
  • Pegg, A. E. (1986). "Recent advances in the biochemistry of polyamines in eukaryotes." Biochem J 234:249-262.3087344
  • Mattheakis, L. C., Shen, W. H., Collier, R. J. (1992). "DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae." Mol Cell Biol 12:4026-4037.1508200
  • Marobbio, C. M., Agrimi, G., Lasorsa, F. M., Palmieri, F. (2003). "Identification and functional reconstitution of yeast mitochondrial carrier for S-adenosylmethionine." EMBO J 22:5975-5982.14609944
  • Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., Sinclair, D. A. (2003). "Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae." Nature 423:181-185.12736687
  • Katz, J. E., Dumlao, D. S., Wasserman, J. I., Lansdown, M. G., Jung, M. E., Faull, K. F., Clarke, S. (2004). "3-Isopropylmalate is the major endogenous substrate of the Saccharomyces cerevisiae trans-aconitate methyltransferase." Biochemistry 43:5976-5986.15147181
  • Marbois, B., Gin, P., Faull, K. F., Poon, W. W., Lee, P. T., Strahan, J., Shepherd, J. N., Clarke, C. F. (2005). "Coq3 and Coq4 define a polypeptide complex in yeast mitochondria for the biosynthesis of coenzyme Q." J Biol Chem 280:20231-20238.15792955
  • Thomas, D., Becker, A., Surdin-Kerjan, Y. (2000). "Reverse methionine biosynthesis from S-adenosylmethionine in eukaryotic cells." J Biol Chem 275:40718-40724.11013242
  • Gary, J. D., Lin, W. J., Yang, M. C., Herschman, H. R., Clarke, S. (1996). "The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae." J Biol Chem 271:12585-12594.8647869
  • Kodaki, T., Yamashita, S. (1987). "Yeast phosphatidylethanolamine methylation pathway. Cloning and characterization of two distinct methyltransferase genes." J Biol Chem 262:15428-15435.2445736
  • Yamashita, S., Nikawa, J. (1997). "Phosphatidylserine synthase from yeast." Biochim Biophys Acta 1348:228-235.9370337
  • Castrillo, J. I., Zeef, L. A., Hoyle, D. C., Zhang, N., Hayes, A., Gardner, D. C., Cornell, M. J., Petty, J., Hakes, L., Wardleworth, L., Rash, B., Brown, M., Dunn, W. B., Broadhurst, D., O'Donoghue, K., Hester, S. S., Dunkley, T. P., Hart, S. R., Swainston, N., Li, P., Gaskell, S. J., Paton, N. W., Lilley, K. S., Kell, D. B., Oliver, S. G. (2007). "Growth control of the eukaryote cell: a systems biology study in yeast." J Biol 6:4.17439666
Synthesis Reference:Not Available
External Links:
ResourceLink
CHEBI ID15414
HMDB IDHMDB01185
Pubchem Compound ID1079
Kegg IDC00019
ChemSpider ID21865164
FOODB IDFDB031152
WikipediaS-Adenosyl_methionine
BioCyc IDS-ADENOSYLMETHIONINE

Enzymes

General function:
Involved in methyltransferase activity
Specific function:
Required for the methylation step in diphthamide biosynthesis
Gene Name:
DPH5
Uniprot ID:
P32469
Molecular weight:
33847.0
Reactions
3 S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine → 3 S-adenosyl-L-homocysteine + 2-(3-carboxy-3-(trimethylammonio)propyl)-L-histidine.
General function:
Involved in methyltransferase activity
Specific function:
Siroheme synthase involved in methionine biosynthesis
Gene Name:
MET1
Uniprot ID:
P36150
Molecular weight:
66124.70313
Reactions
S-adenosyl-L-methionine + uroporphyrinogen III → S-adenosyl-L-homocysteine + precorrin-1.
S-adenosyl-L-methionine + precorrin-1 → S-adenosyl-L-homocysteine + precorrin-2.
General function:
Involved in acyltransferase activity
Specific function:
Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria
Gene Name:
CAT2
Uniprot ID:
P32796
Molecular weight:
77241.20313
Reactions
Acetyl-CoA + carnitine → CoA + O-acetylcarnitine.
General function:
Involved in acyltransferase activity
Specific function:
Involved in the transfer of acetyl-CoA into mitochondria. May also be involved in the metabolism of acetate and of ethanol
Gene Name:
YAT1
Uniprot ID:
P80235
Molecular weight:
77764.79688
Reactions
Acetyl-CoA + carnitine → CoA + O-acetylcarnitine.
General function:
Involved in acyltransferase activity
Specific function:
Involved in the shutteling of acetyl-CoA in the cell
Gene Name:
YAT2
Uniprot ID:
P40017
Molecular weight:
103333.0
Reactions
Acetyl-CoA + carnitine → CoA + O-acetylcarnitine.
General function:
Involved in methyltransferase activity
Specific function:
Non-specific O-methyltransferase that catalyzes the 2 O- methylation steps in the ubiquinone biosynthetic pathway
Gene Name:
COQ3
Uniprot ID:
P27680
Molecular weight:
36330.60156
Reactions
S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate → S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans-polyprenylbenzoate.
S-adenosyl-L-methionine + 3-demethylubiquinone-n → S-adenosyl-L-homocysteine + ubiquinone-n.
S-adenosyl-L-methionine + 2-hexaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinol → S-adenosyl-L-homocysteine + ubiquinol.
General function:
Involved in catalytic activity
Specific function:
Dethiobiotin + sulfur + 2 S-adenosyl-L- methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosine
Gene Name:
BIO2
Uniprot ID:
P32451
Molecular weight:
41883.80078
Reactions
Dethiobiotin + sulfur + 2 S-adenosyl-L-methionine → biotin + 2 L-methionine + 2 5'-deoxyadenosine.
General function:
Involved in transaminase activity
Specific function:
Catalyzes the transfer of the alpha-amino group from S- adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor
Gene Name:
BIO3
Uniprot ID:
P50277
Molecular weight:
53708.39844
Reactions
S-adenosyl-L-methionine + 8-amino-7-oxononanoate → S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate.
General function:
Involved in methionine adenosyltransferase activity
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP
Gene Name:
SAM1
Uniprot ID:
P10659
Molecular weight:
41818.0
Reactions
ATP + L-methionine + H(2)O → phosphate + diphosphate + S-adenosyl-L-methionine.
General function:
Involved in catalytic activity
Specific function:
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (Probable)
Gene Name:
LIP5
Uniprot ID:
P32875
Molecular weight:
46246.80078
Reactions
Protein N(6)-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine → protein N(6)-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine.
General function:
Involved in methyltransferase activity
Specific function:
Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate and 3-isopropylmalate at high affinity and of other molecules like cis-aconitate, isocitrate, and citrate at lower velocities and affinities. The function of trans-aconitate methylation appears to be in reducing the toxicity of this spontaneous breakdown product of cis-aconitate. The role of 3-isopropylmalate methylation is unclear but may represent a metabolic branch at 3-isopropylmalate, where some of the material is taken in the pathway leading to leucine and some is taken in a pathway to the 3-isopropylmalate methyl ester, a molecule that provides a signal to switch from vegetative to invasive growth in response to amino acid starvation
Gene Name:
TMT1
Uniprot ID:
P32643
Molecular weight:
34768.0
Reactions
S-adenosyl-L-methionine + trans-aconitate → S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate.
General function:
Involved in adenosylmethionine decarboxylase activity
Specific function:
S-adenosylmethionine decarboxylase is essential for normal growth, sporulation, maintenance of ds-RNA virus, biosynthesis of spermine and spermidine
Gene Name:
SPE2
Uniprot ID:
P21182
Molecular weight:
46232.0
Reactions
S-adenosyl-L-methionine → (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2).
General function:
Involved in ubiquinone biosynthetic process
Specific function:
Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of COQ3, COQ4, COQ6, COQ7 and COQ9 polypeptides
Gene Name:
COQ4
Uniprot ID:
O13525
Molecular weight:
38626.80078
General function:
Involved in [cytochrome c]-lysine N-methyltransferase a
Specific function:
Methyltransferase which mediates trimethylation of Lys- 77 of cytochrome c (CYC1)
Gene Name:
CTM1
Uniprot ID:
P38818
Molecular weight:
68283.60156
Reactions
S-adenosyl-L-methionine + [cytochrome c]-L-lysine → S-adenosyl-L-homocysteine + [cytochrome c]-N(6)-methyl-L-lysine.
General function:
Involved in methyltransferase activity
Specific function:
Catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNAs
Gene Name:
TRM10
Uniprot ID:
Q12400
Molecular weight:
34520.19922
Reactions
S-adenosyl-L-methionine + tRNA → S-adenosyl-L-homocysteine + tRNA containing N(1)-methylguanine.
General function:
Involved in tRNA (adenine-N1-)-methyltransferase activity
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. GCD14 is also required for repression of GCN4 mRNA translation by the upstream open reading frames (uORFs) under conditions of amino acid sufficiency
Gene Name:
GCD14
Uniprot ID:
P46959
Molecular weight:
43919.30078
Reactions
S-adenosyl-L-methionine + tRNA → S-adenosyl-L-homocysteine + tRNA containing N(1)-methyladenine.
General function:
Involved in protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity
Specific function:
Mediates C-terminal methylation of the isoprenylated C- terminal cysteine in A-factor mating pheromone and Ras proteins
Gene Name:
STE14
Uniprot ID:
P32584
Molecular weight:
27887.40039
Reactions
S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine → S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester.
General function:
Involved in protein methyltransferase activity
Specific function:
Methylates arginines in a variety of RNA-binding proteins. Methylates NOP3. Can catalyze both the mono- and asymmetric dimethylation
Gene Name:
HMT1
Uniprot ID:
P38074
Molecular weight:
39785.80078
Reactions
General function:
Involved in homocysteine S-methyltransferase activity
Specific function:
Homocysteine S-methyltransferase involved in the conversion of S-adenosylmethionine (AdoMet) to methionine to control the methionine/AdoMet ratio. Converts also S- methylmethionine (SMM) to methionine
Gene Name:
MHT1
Uniprot ID:
Q12525
Molecular weight:
36714.5
Reactions
S-methyl-L-methionine + L-homocysteine → 2 L-methionine.
General function:
Involved in tRNA (guanine-N7-)-methyltransferase activity
Specific function:
Methyltransferase that catalyzes the formation of N(7)- methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity
Gene Name:
TRM8
Uniprot ID:
Q12009
Molecular weight:
33391.19922
Reactions
S-adenosyl-L-methionine + tRNA → S-adenosyl-L-homocysteine + tRNA containing N(7)-methylguanine.
General function:
Involved in homocysteine S-methyltransferase activity
Specific function:
Homocysteine S-methyltransferase involved in the conversion of S-adenosylmethionine (AdoMet) to methionine to control the methionine/AdoMet ratio. Converts also S- methylmethionine (SMM) to methionine
Gene Name:
SAM4
Uniprot ID:
Q08985
Molecular weight:
36668.19922
Reactions
S-methyl-L-methionine + L-homocysteine → 2 L-methionine.
General function:
Involved in nicotinamide N-methyltransferase activity
Specific function:
Putative nicotinamide N-methyltransferase involved in rDNA silencing and in lifespan determination
Gene Name:
NNT1
Uniprot ID:
Q05874
Molecular weight:
29632.30078
Reactions
S-adenosyl-L-methionine + nicotinamide → S-adenosyl-L-homocysteine + 1-methylnicotinamide.
General function:
Involved in phosphatidylethanolamine N-methyltransferas
Specific function:
S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
Gene Name:
PEM1
Uniprot ID:
P05374
Molecular weight:
101203.0
Reactions
S-adenosyl-L-methionine + phosphatidylethanolamine → S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine.
General function:
Involved in identical protein binding
Specific function:
Specifically methylates guanosine-37 in various tRNAs. Not dependent on the nature of the nucleoside 5' of the target nucleoside
Gene Name:
TRM5
Uniprot ID:
P38793
Molecular weight:
56514.0
Reactions
S-adenosyl-L-methionine + tRNA → S-adenosyl-L-homocysteine + tRNA containing N(1)-methylguanine.
General function:
Involved in N-methyltransferase activity
Specific function:
S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid methylene fatty acid
Gene Name:
OPI3
Uniprot ID:
P05375
Molecular weight:
23150.09961
Reactions
S-adenosyl-L-methionine + phospholipid olefinic fatty acid → S-adenosyl-L-homocysteine + phospholipid methylene fatty acid.
General function:
Involved in methyltransferase activity
Specific function:
Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol
Gene Name:
ERG6
Uniprot ID:
P25087
Molecular weight:
43430.5
Reactions
S-adenosyl-L-methionine + 5-alpha-cholesta-8,24-dien-3-beta-ol → S-adenosyl-L-homocysteine + 24-methylene-5-alpha-cholest-8-en-3-beta-ol.
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2- thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base
Gene Name:
SLM3
Uniprot ID:
Q12093
Molecular weight:
47048.80078
Reactions
S-adenosyl-L-methionine + tRNA containing 5-aminomethyl-2-thiouridylate → S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate
General function:
Coenzyme transport and metabolism
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP
Gene Name:
SAM2
Uniprot ID:
P19358
Molecular weight:
42255.5
Reactions
ATP + L-methionine + H(2)O → phosphate + diphosphate + S-adenosyl-L-methionine.
General function:
Involved in RNA methyltransferase activity
Specific function:
Catalyzes the formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNA. May also have a role in tRNA stabilization or maturation
Gene Name:
TRM2
Uniprot ID:
P33753
Molecular weight:
72851.79688
Reactions
S-adenosyl-L-methionine + tRNA containing uridine at position 54 → S-adenosyl-L-homocysteine + tRNA containing ribothymidine at position 54.
General function:
Involved in histone-lysine N-methyltransferase activity
Specific function:
Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. Can bind to DNA (in vitro)
Gene Name:
DOT1
Uniprot ID:
Q04089
Molecular weight:
66200.70313
Reactions
S-adenosyl-L-methionine + L-lysine-[histone] → S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
General function:
Involved in histone-lysine N-methyltransferase activity
Specific function:
Histone methyltransferase that methylates histone H3 to form H3K36me. Involved in transcription elongation as well as in transcription repression. The methyltransferase activity requires the recruitment to the RNA polymerase II, which is CTK1 dependent
Gene Name:
SET2
Uniprot ID:
P46995
Molecular weight:
84538.79688
Reactions
S-adenosyl-L-methionine + L-lysine-[histone] → S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
General function:
Involved in histone-lysine N-methyltransferase activity
Specific function:
Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation
Gene Name:
SET1
Uniprot ID:
P38827
Molecular weight:
123911.0
Reactions
S-adenosyl-L-methionine + L-lysine-[histone] → S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].

Transporters

General function:
Involved in transport
Specific function:
High-affinity S-adenosylmethionine permease, required for utilization of S-adenosylmethionine as a sulfur source
Gene Name:
SAM3
Uniprot ID:
Q08986
Molecular weight:
64353.0
General function:
Involved in binding
Specific function:
Not Available
Gene Name:
PET8
Uniprot ID:
P38921
Molecular weight:
31026.59961