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Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2014-10-29 21:49:14 UTC
HMDB IDHMDB00696
Secondary Accession NumbersNone
Metabolite Identification
Common NameL-Methionine
DescriptionMethionine is a dietary indispensable amino acid required for normal growth and development of humans, other mammals, and avian species. In addition to being a substrate for protein synthesis, it is an intermediate in transmethylation reactions, serving as the major methyl group donor in vivo, including the methyl groups for DNA and RNA intermediates. Methionine is a methyl acceptor for 5-methyltetrahydrofolate-homocysteine methyl transferase (methionine synthase), the only reaction that allows for the recycling of this form of folate, and is also a methyl acceptor for the catabolism of betaine. Methionine is also required for synthesis of cysteine. Methionine is accepted as the metabolic precursor for cysteine. Only the sulfur atom from methionine is transferred to cysteine; the carbon skeleton of cysteine is donated by serine. (PMID 16702340 ). The adequacy range of dietary requirements of specific amino acids in disease states is difficult to determine. Requirements may not be similar in disease with regard to protein synthesis. Requirements for this purpose can be assessed only when such a function can be measured and related to clinical outcome. There is apparent consensus concerning normal sulfur amino acid (SAA) requirements. WHO recommendations amount to 13 mg/kg per 24 h in healthy adults. This amount is roughly doubled in artificial nutrition regimens. In disease or after trauma, requirements may be altered for methionine, cysteine, and taurine. Although in specific cases of congenital enzyme deficiency, prematurity, or diminished liver function, hypermethionemia or hyperhomocysteinemia may occur, SAA supplementation can be considered safe in amounts exceeding 2-3 times the minimal recommended daily intake. Apart from some very specific indications (e.g., acetaminophen poisoning) the usefulness of SAA supplementation is not yet established.(PMID 16702341 ). Methionine is known to exacerbate psychopathological symptoms in schizophrenic patients, there is no evidence of similar effects in healthy subjects. The role of methionine as a precursor of homocysteine is the most notable cause for concern. A "loading dose" of methionine (0.1 g/kg) has been given, and the resultant acute increase in plasma homocysteine has been used as an index of the susceptibility to cardiovascular disease. Although this procedure results in vascular dysfunction, this is acute and unlikely to result in permanent damage. However, a 10-fold larger dose, given mistakenly, resulted in death. Longer-term studies in adults have indicated no adverse consequences of moderate fluctuations in dietary methionine intake, but intakes higher than 5 times normal resulted in elevated homocysteine levels. These effects of methionine on homocysteine and vascular function are moderated by supplements of vitamins B-6, B-12, C, and folic acid. In infants, methionine intakes of 2 to 5 times normal resulted in impaired growth and extremely high plasma methionine levels, but no adverse long-term consequences were observed. (PMID 16702346 ).
Structure
Thumb
Synonyms
  1. (2S)-2-amino-4-(methylsulfanyl)butanoate
  2. (2S)-2-amino-4-(methylsulfanyl)butanoic acid
  3. (L)-methionine
  4. (S)-(+)-methionine
  5. (S)-2-amino-4-(methylthio)-Butanoate
  6. (S)-2-amino-4-(methylthio)-Butanoic acid
  7. (S)-2-Amino-4-(methylthio)butanoate
  8. (S)-2-Amino-4-(methylthio)butanoic acid
  9. (S)-2-amino-4-(methylthio)butyric acid
  10. (S)-methionine
  11. 2-Amino-4-(methylthio)butyrate
  12. 2-Amino-4-(methylthio)butyric acid
  13. 2-Amino-4-methylthiobutanoate
  14. 2-Amino-4-methylthiobutanoic acid
  15. A-Amino-g-methylmercaptobutyrate
  16. A-Amino-g-methylmercaptobutyric acid
  17. Acimethin
  18. alpha-Amino-alpha-aminobutyric acid
  19. alpha-Amino-gamma-methylmercaptobutyrate
  20. alpha-Amino-gamma-methylmercaptobutyric acid
  21. Cymethion
  22. G-Methylthio-a-aminobutyrate
  23. G-Methylthio-a-aminobutyric acid
  24. gamma-Methylthio-alpha-aminobutyrate
  25. gamma-Methylthio-alpha-aminobutyric acid
  26. H-Met-h
  27. H-Met-oh
  28. L(-)-Amino-alpha-amino-alpha-aminobutyric acid
  29. L(-)-Amino-gamma-methylthiobutyric acid
  30. L-(-)-Methionine
  31. L-2-Amino-4-(methylthio)butyric acid
  32. L-2-Amino-4-methylthiobutyric acid
  33. L-a-Amino-g-methylthiobutyrate
  34. L-a-Amino-g-methylthiobutyric acid
  35. L-alpha-Amino-gamma-methylmercaptobutyric acid
  36. L-alpha-Amino-gamma-methylthiobutyrate
  37. L-alpha-Amino-gamma-methylthiobutyric acid
  38. L-gamma-Methylthio-alpha-aminobutyric acid
  39. L-Methionin
  40. L-Methionine
  41. L-Methioninum
  42. Liquimeth
  43. Mepron
  44. MET
  45. Methilanin
  46. Methionine
  47. Methioninum
  48. Metionina
  49. Neo-methidin
  50. Poly-L-methionine
  51. Polymethionine
  52. S-Methionine
  53. S-Methyl-L-homocysteine
  54. Toxin WAR
Chemical FormulaC5H11NO2S
Average Molecular Weight149.211
Monoisotopic Molecular Weight149.051049291
IUPAC Name(2S)-2-amino-4-(methylsulfanyl)butanoic acid
Traditional NameL-methionine
CAS Registry Number63-68-3
SMILES
CSCC[C@H](N)C(O)=O
InChI Identifier
InChI=1S/C5H11NO2S/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-/m0/s1
InChI KeyFFEARJCKVFRZRR-BYPYZUCNSA-N
Chemical Taxonomy
KingdomOrganic Compounds
Super ClassAmino Acids, Peptides, and Analogues
ClassAmino Acids and Derivatives
Sub ClassAlpha Amino Acids and Derivatives
Other Descriptors
  • Aliphatic Acyclic Compounds
  • Common amino acids(KEGG)
  • amino acid zwitterion(ChEBI)
Substituents
  • Carboxylic Acid
  • Primary Aliphatic Amine (Alkylamine)
  • Thioether
Direct ParentAlpha Amino Acids and Derivatives
Ontology
StatusDetected and Quantified
Origin
  • Drug metabolite
  • Food
Biofunction
  • Component of Aminoacyl-tRNA biosynthesis
  • Component of Glycine, serine and threonine metabolism
  • Component of Histidine metabolism
  • Component of Methionine metabolism
  • Component of Selenoamino acid metabolism
  • Component of Tyrosine metabolism
  • Essential amino acids
  • Waste products
ApplicationNot Available
Cellular locations
  • Extracellular
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point284 °CNot Available
Boiling PointNot AvailableNot Available
Water Solubility56.6 mg/mLYALKOWSKY,SH & DANNENFELSER,RM (1992)
LogP-1.87HANSCH,C ET AL. (1995)
Predicted Properties
PropertyValueSource
Water Solubility23.9 g/LALOGPS
logP-1.9ALOGPS
logP-2.2ChemAxon
logS-0.8ALOGPS
pKa (Strongest Acidic)2.53ChemAxon
pKa (Strongest Basic)9.5ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area63.32ChemAxon
Rotatable Bond Count4ChemAxon
Refractivity37.59ChemAxon
Polarizability15.5ChemAxon
Spectra
SpectraGC-MSMS/MSLC-MS1D NMR2D NMR
Biological Properties
Cellular Locations
  • Extracellular
Biofluid Locations
  • Blood
  • Cerebrospinal Fluid (CSF)
  • Saliva
  • Urine
Tissue Location
  • Fibroblasts
  • Kidney
  • Liver
  • Muscle
  • Pancreas
  • Prostate
  • Spleen
Pathways
NameSMPDB LinkKEGG Link
Betaine MetabolismSMP00123map00260
Glycine and Serine MetabolismSMP00004map00260
Methionine MetabolismSMP00033map00270
Spermidine and Spermine BiosynthesisSMP00445Not Available
Transcription/TranslationSMP00019Not Available
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified25.0 (21.0-29.0) uMAdult (>18 years old)BothNormal details
BloodDetected and Quantified33.4 +/- 9 uMAdult (>18 years old)Not SpecifiedNormal details
BloodDetected and Quantified35.0 +/- 5.0 uMNewborn (0-30 days old)Not SpecifiedNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified27.0 +/- 5.0 uMChildren (1-13 years old)MaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified32.0 +/- 6.0 uMAdult (>18 years old)MaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified27.0 +/- 5.0 uMAdult (>18 years old)FemaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified20.00 (10.00-30.00) uMAdult (>18 years old)BothNormal details
BloodDetected and Quantified29.8 +/- 6.3 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified5 +/- 4 uMNot SpecifiedBothNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified3.6 +/- 0.98 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified2.9 +/- 0.69 uMAdult (>18 years old)BothNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified1.9 +/- 0.7 uMAdult (>18 years old)BothNormal
    • Geigy Scientific ...
details
Cerebrospinal Fluid (CSF)Detected and Quantified6.1 +/- 3.1 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified4.3 +/- 2.5 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified4.07 (3.00-5.14) uMAdult (>18 years old)BothNormal details
SalivaDetected and Quantified0.0354 +/- 0.0873 uMAdult (>18 years old)Female
Normal
    • Sugimoto et al. (...
details
SalivaDetected and Quantified0.176 +/- 0.152 uMAdult (>18 years old)Female
Normal
    • Sugimoto et al. (...
details
SalivaDetected and Quantified2.88 +/- 5.55 uMAdult (>18 years old)Male
Normal
    • Sugimoto et al. (...
details
SalivaDetected and Quantified0.418 +/- 0.420 uMAdult (>18 years old)Both
Normal
    • Sugimoto et al. (...
details
SalivaDetected and Quantified8.81 +/- 5.94 uMAdult (>18 years old)BothNormal
    • Dame, ZT. et al. ...
details
UrineDetected and Quantified1.0 umol/mmol creatinineAdult (>18 years old)BothNormal details
UrineDetected and Quantified2.303 (0.658-3.947) umol/mmol creatinineAdult (>18 years old)BothNormal
    details
    UrineDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
    Normal
    details
    UrineDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
    Normal
    details
    UrineDetected and Quantified1.70 +/- 1.01 umol/mmol creatinineAdult (>18 years old)BothNormal details
    UrineDetected and Quantified0.065 (0.0-0.13) umol/mmol creatinineNewborn (0-30 days old)BothNormal
      • Geigy Scientific ...
      • West Cadwell, N.J...
      • Basel, Switzerlan...
    details
    UrineDetected and Quantified0.8 (0.4-1.6) umol/mmol creatinineAdult (>18 years old)Both
    Normal
    details
    UrineDetected and Quantified0.611 +/- 0.45 umol/mmol creatinineChildren (1-13 years old)MaleNormal
      • Geigy Scientific ...
      • West Cadwell, N.J...
      • Basel, Switzerlan...
    details
    UrineDetected and Quantified1.3 +/- 0.97 umol/mmol creatinineAdult (>18 years old)MaleNormal
      • Geigy Scientific ...
      • West Cadwell, N.J...
      • Basel, Switzerlan...
    details
    UrineDetected and Quantified1.12 +/- 0.97 umol/mmol creatinineAdult (>18 years old)FemaleNormal
      • Geigy Scientific ...
      • West Cadwell, N.J...
      • Basel, Switzerlan...
    details
    UrineDetected and Quantified1.4 (0.5-2.5) umol/mmol creatinineAdult (>18 years old)Both
    Normal
    details
    UrineDetected and Quantified0.4 umol/mmol creatinineAdult (>18 years old)BothNormal details
    UrineDetected and Quantified1.21 +/- 1.20 umol/mmol creatinineInfant (0-1 year old)BothNormal details
    Abnormal Concentrations
    BiofluidStatusValueAgeSexConditionReferenceDetails
    BloodDetected and Quantified17.8 (17.0-18.6) uMAdult (>18 years old)Both
    Epilepsy
    details
    BloodDetected and Quantified775.00 (250.00-1300.00) uMChildren (1-13 years old)BothMethionine adenosyl transferase deficiency details
    BloodDetected and Quantified17.3 +/- 9.5 uMAdult (>18 years old)Not SpecifiedHeart Transplant details
    BloodDetected and Quantified518.5 (37.00-1000.00) uMChildren (1-13 years old)BothS-Adenosylhomocysteine hydrolase deficiency details
    BloodDetected and Quantified750.0 (500.00-1000.00) uMChildren (1-13 years old)BothGlycine N-Methyltransferase deficiency details
    BloodDetected and Quantified9.00 (0.00-18.00) uMChildren (1-13 years old)BothHomocystinuria details
    BloodDetected and Quantified415.0 +/- 7.0 uMAdult (>18 years old)Both
    Heart failure
    details
    Cerebrospinal Fluid (CSF)Detected and Quantified2.7 +/- 0.67 uMAdult (>18 years old)BothSchizophrenia details
    Cerebrospinal Fluid (CSF)Detected and Quantified6.0 +/- 5.3 uMChildren (1-13 years old)Not SpecifiedLeukemia details
    Cerebrospinal Fluid (CSF)Detected and Quantified3.5 +/- 0.4 uMChildren (1-13 years old)Not Specified
    Leukemia
    details
    Associated Disorders and Diseases
    Disease References
    Epilepsy
    1. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. Pubmed: 14992292
    Schizophrenia
    1. Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. Pubmed: 7595563
    Heart failure
    1. Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. Pubmed: 16789974
    Homocystinuria
    1. MetaGene
    Hypermethioninemia
    1. MetaGene
    Leukemia
    1. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. Pubmed: 15911239
    Methionine adenosyltransferase deficiency
    1. MetaGene
    Glycine N-methyltransferase deficiency
    1. MetaGene
    Homocystinuria due to defect of N(5,10)-methylene THF deficiency
    1. MetaGene
    Associated OMIM IDs
    • 181500 (Schizophrenia)
    • 606664 (Glycine N-methyltransferase deficiency)
    • 236250 (Homocystinuria due to defect of N(5,10)-methylene THF deficiency)
    • 236200 (Homocystinuria)
    • 250850 (Methionine adenosyltransferase deficiency)
    • 613752 (Hypermethioninemia)
    DrugBank IDDB00134
    DrugBank Metabolite IDDBMET00506
    Phenol Explorer Compound IDNot Available
    Phenol Explorer Metabolite IDNot Available
    FoodDB IDFDB012683
    KNApSAcK IDC00001379
    Chemspider ID5907
    KEGG Compound IDC00073
    BioCyc IDMET
    BiGG ID33753
    Wikipedia LinkMET
    NuGOwiki LinkHMDB00696
    Metagene LinkHMDB00696
    METLIN ID5664
    PubChem Compound6137
    PDB IDMET
    ChEBI ID16643
    References
    Synthesis ReferenceBoy, Matthias; Klein, Daniela; Schroeder, Hartwig. Method for the production and recovery of methionine. PCT Int. Appl. (2005), 34 pp.
    Material Safety Data Sheet (MSDS)Download (PDF)
    General References
    1. Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. Pubmed: 19212411
    2. Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. Pubmed: 2026685
    3. Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. Pubmed: 12834252
    4. Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. Pubmed: 6198473
    5. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. Pubmed: 15911239
    6. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. Pubmed: 12297216
    7. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. Pubmed: 14992292
    8. Kersemans V, Cornelissen B, Kersemans K, Bauwens M, Achten E, Dierckx RA, Mertens J, Slegers G: In vivo characterization of 123/125I-2-iodo-L-phenylalanine in an R1M rhabdomyosarcoma athymic mouse model as a potential tumor tracer for SPECT. J Nucl Med. 2005 Mar;46(3):532-9. Pubmed: 15750170
    9. Alme B, Bremmelgaard A, Sjovall J, Thomassen P: Analysis of metabolic profiles of bile acids in urine using a lipophilic anion exchanger and computerized gas-liquid chromatorgaphy-mass spectrometry. J Lipid Res. 1977 May;18(3):339-62. Pubmed: 864325
    10. Sardharwalla IB, Fowler B, Robins AJ, Komrower GM: Detection of heterozygotes for homocystinuria. Study of sulphur-containing amino acids in plasma and urine after L-methionine loading. Arch Dis Child. 1974 Jul;49(7):553-9. Pubmed: 4851308
    11. Alton KB, Hernandez A, Alvarez N, Patrick JE: High-performance liquid chromatographic determination of N-[2(S)-(mercaptomethyl)-3-(2-methylphenyl)-1-oxopropyl]-L-methionine, the active plasma metabolite of a prodrug atriopeptidase inhibitor (SCH 42495), using a thiol selective (Au/Hg) amperometric detector. J Chromatogr. 1992 Sep 2;579(2):307-17. Pubmed: 1429978
    12. Fischer JL, Lancia JK, Mathur A, Smith ML: Selenium protection from DNA damage involves a Ref1/p53/Brca1 protein complex. Anticancer Res. 2006 Mar-Apr;26(2A):899-904. Pubmed: 16619485
    13. Ditscheid B, Funfstuck R, Busch M, Schubert R, Gerth J, Jahreis G: Effect of L-methionine supplementation on plasma homocysteine and other free amino acids: a placebo-controlled double-blind cross-over study. Eur J Clin Nutr. 2005 Jun;59(6):768-75. Pubmed: 15870821
    14. Hesse A, Heimbach D: Causes of phosphate stone formation and the importance of metaphylaxis by urinary acidification: a review. World J Urol. 1999 Oct;17(5):308-15. Pubmed: 10552150
    15. Harth G, Horwitz MA: Inhibition of Mycobacterium tuberculosis glutamine synthetase as a novel antibiotic strategy against tuberculosis: demonstration of efficacy in vivo. Infect Immun. 2003 Jan;71(1):456-64. Pubmed: 12496196
    16. Takasu A, Shimosegawa T, Shimosegawa E, Hatazawa J, Kimura K, Fujita M, Koizumi M, Kanno I, Toyota T: 11C-methionine uptake to the pancreas and its secretion: a positron emission tomography study in humans. Pancreas. 1999 May;18(4):392-8. Pubmed: 10231845
    17. Ball RO, Courtney-Martin G, Pencharz PB: The in vivo sparing of methionine by cysteine in sulfur amino acid requirements in animal models and adult humans. J Nutr. 2006 Jun;136(6 Suppl):1682S-1693S. Pubmed: 16702340
    18. van de Poll MC, Dejong CH, Soeters PB: Adequate range for sulfur-containing amino acids and biomarkers for their excess: lessons from enteral and parenteral nutrition. J Nutr. 2006 Jun;136(6 Suppl):1694S-1700S. Pubmed: 16702341
    19. Garlick PJ: Toxicity of methionine in humans. J Nutr. 2006 Jun;136(6 Suppl):1722S-1725S. Pubmed: 16702346

    Enzymes

    General function:
    Involved in cobalamin binding
    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:
    Q99707
    Molecular weight:
    140525.91
    Reactions
    5-Methyltetrahydrofolic acid + Homocysteine → Tetrahydrofolic acid + L-Methioninedetails
    References
    1. Taurog RE, Matthews RG: Activation of methyltetrahydrofolate by cobalamin-independent methionine synthase. Biochemistry. 2006 Apr 25;45(16):5092-102. Pubmed: 16618098
    2. Hughes JA: In vivo hydrolysis of S-adenosyl-L-methionine in Escherichia coli increases export of 5-methylthioribose. Can J Microbiol. 2006 Jun;52(6):599-602. Pubmed: 16788729
    3. Reynolds E: Vitamin B12, folic acid, and the nervous system. Lancet Neurol. 2006 Nov;5(11):949-60. Pubmed: 17052662
    4. Banks EC, Doughty SW, Toms SM, Wheelhouse RT, Nicolaou A: Inhibition of cobalamin-dependent methionine synthase by substituted benzo-fused heterocycles. FEBS J. 2007 Jan;274(1):287-99. Pubmed: 17222188
    5. Yamada K, Kawata T, Wada M, Mori K, Tamai H, Tanaka N, Tadokoro T, Tobimatsu T, Toraya T, Maekawa A: Testicular injury to rats fed on soybean protein-based vitamin B12-deficient diet can be reduced by methionine supplementation. J Nutr Sci Vitaminol (Tokyo). 2007 Apr;53(2):95-101. Pubmed: 17615995
    General function:
    Involved in methylenetetrahydrofolate reductase (NADPH) activity
    Specific function:
    Catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co-substrate for homocysteine remethylation to methionine.
    Gene Name:
    MTHFR
    Uniprot ID:
    P42898
    Molecular weight:
    74595.895
    References
    1. Lor KL, Cossins EA: Regulation of C metabolism by L-methionine in Saccharomyces cerevisiae. Biochem J. 1972 Dec;130(3):773-83. Pubmed: 4198357
    General function:
    Involved in 1-aminocyclopropane-1-carboxylate synthase activity
    Specific function:
    Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity towards phenylalanine.
    Gene Name:
    TAT
    Uniprot ID:
    P17735
    Molecular weight:
    50398.895
    Reactions
    2-Oxo-4-methylthiobutanoic acid + L-Glutamic acid → L-Methionine + Oxoglutaric aciddetails
    General function:
    Involved in methionine adenosyltransferase activity
    Specific function:
    Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
    Gene Name:
    MAT2A
    Uniprot ID:
    P31153
    Molecular weight:
    43660.37
    Reactions
    Adenosine triphosphate + L-Methionine + Water → Phosphoric acid + Pyrophosphate + S-Adenosylmethioninedetails
    Phosphoric acid + Pyrophosphate + S-Adenosylmethionine → Adenosine triphosphate + L-Methionine + Waterdetails
    References
    1. Rodriguez JL, Boukaba A, Sandoval J, Georgieva EI, Latasa MU, Garcia-Trevijano ER, Serviddio G, Nakamura T, Avila MA, Sastre J, Torres L, Mato JM, Lopez-Rodas G: Transcription of the MAT2A gene, coding for methionine adenosyltransferase, is up-regulated by E2F and Sp1 at a chromatin level during proliferation of liver cells. Int J Biochem Cell Biol. 2007;39(4):842-50. Epub 2007 Jan 20. Pubmed: 17317269
    2. Yang H, Magilnick N, Noureddin M, Mato JM, Lu SC: Effect of hepatocyte growth factor on methionine adenosyltransferase genes and growth is cell density-dependent in HepG2 cells. J Cell Physiol. 2007 Mar;210(3):766-73. Pubmed: 17154373
    3. Lin WC, Lin WL: Ameliorative effect of Ganoderma lucidum on carbon tetrachloride-induced liver fibrosis in rats. World J Gastroenterol. 2006 Jan 14;12(2):265-70. Pubmed: 16482628
    4. Chen H, Xia M, Lin M, Yang H, Kuhlenkamp J, Li T, Sodir NM, Chen YH, Josef-Lenz H, Laird PW, Clarke S, Mato JM, Lu SC: Role of methionine adenosyltransferase 2A and S-adenosylmethionine in mitogen-induced growth of human colon cancer cells. Gastroenterology. 2007 Jul;133(1):207-18. Epub 2007 Apr 11. Pubmed: 17631143
    General function:
    Involved in methyltransferase activity
    Specific function:
    Catalyzes the transfer of a methyl group from AdoMet to trivalent arsenicals producing methylated and dimethylated arsenicals. It methylates arsenite to form methylarsonate, Me-AsO(3)H(2), which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite is also a substrate and it is converted into the much less toxic compound dimethylarsinate (cacodylate), Me(2)As(O)-OH (By similarity).
    Gene Name:
    AS3MT
    Uniprot ID:
    Q9HBK9
    Molecular weight:
    41747.49
    General function:
    Involved in methyltransferase activity
    Specific function:
    Functions as thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds (By similarity). Catalyzes the N-methylation of tryptamine and structurally related compounds.
    Gene Name:
    INMT
    Uniprot ID:
    O95050
    Molecular weight:
    28833.695
    General function:
    Involved in methionine adenosyltransferase activity
    Specific function:
    Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
    Gene Name:
    MAT1A
    Uniprot ID:
    Q00266
    Molecular weight:
    43647.6
    Reactions
    Adenosine triphosphate + L-Methionine + Water → Phosphoric acid + Pyrophosphate + S-Adenosylmethioninedetails
    Phosphoric acid + Pyrophosphate + S-Adenosylmethionine → Adenosine triphosphate + L-Methionine + Waterdetails
    References
    1. Linnebank M, Lagler F, Muntau AC, Roschinger W, Olgemoller B, Fowler B, Koch HG: Methionine adenosyltransferase (MAT) I/III deficiency with concurrent hyperhomocysteinaemia: two novel cases. J Inherit Metab Dis. 2005;28(6):1167-8. Pubmed: 16435220
    2. Yang H, Magilnick N, Noureddin M, Mato JM, Lu SC: Effect of hepatocyte growth factor on methionine adenosyltransferase genes and growth is cell density-dependent in HepG2 cells. J Cell Physiol. 2007 Mar;210(3):766-73. Pubmed: 17154373
    3. Chen H, Xia M, Lin M, Yang H, Kuhlenkamp J, Li T, Sodir NM, Chen YH, Josef-Lenz H, Laird PW, Clarke S, Mato JM, Lu SC: Role of methionine adenosyltransferase 2A and S-adenosylmethionine in mitogen-induced growth of human colon cancer cells. Gastroenterology. 2007 Jul;133(1):207-18. Epub 2007 Apr 11. Pubmed: 17631143
    4. Rodriguez JL, Boukaba A, Sandoval J, Georgieva EI, Latasa MU, Garcia-Trevijano ER, Serviddio G, Nakamura T, Avila MA, Sastre J, Torres L, Mato JM, Lopez-Rodas G: Transcription of the MAT2A gene, coding for methionine adenosyltransferase, is up-regulated by E2F and Sp1 at a chromatin level during proliferation of liver cells. Int J Biochem Cell Biol. 2007;39(4):842-50. Epub 2007 Jan 20. Pubmed: 17317269
    5. Prudova A, Bauman Z, Braun A, Vitvitsky V, Lu SC, Banerjee R: S-adenosylmethionine stabilizes cystathionine beta-synthase and modulates redox capacity. Proc Natl Acad Sci U S A. 2006 Apr 25;103(17):6489-94. Epub 2006 Apr 13. Pubmed: 16614071
    General function:
    Involved in oxidoreductase activity
    Specific function:
    Involved in the reductive regeneration of cob(I)alamin cofactor required for the maintenance of methionine synthase in a functional state.
    Gene Name:
    MTRR
    Uniprot ID:
    Q9UBK8
    Molecular weight:
    77672.995
    References
    1. Kim DJ, Park BL, Koh JM, Kim GS, Kim LH, Cheong HS, Shin HD, Hong JM, Kim TH, Shin HI, Park EK, Kim SY: Methionine synthase reductase polymorphisms are associated with serum osteocalcin levels in postmenopausal women. Exp Mol Med. 2006 Oct 31;38(5):519-24. Pubmed: 17079868
    2. Tvedegaard KC, Rudiger NS, Pedersen BN, Moller J: Detection of MTRR 66A-->G polymorphism using the real-time polymerase chain reaction machine LightCycler for determination of composition of allele after restriction cleavage. Scand J Clin Lab Invest. 2006;66(8):685-93. Pubmed: 17101561
    3. Elmore CL, Wu X, Leclerc D, Watson ED, Bottiglieri T, Krupenko NI, Krupenko SA, Cross JC, Rozen R, Gravel RA, Matthews RG: Metabolic derangement of methionine and folate metabolism in mice deficient in methionine synthase reductase. Mol Genet Metab. 2007 May;91(1):85-97. Epub 2007 Mar 21. Pubmed: 17369066
    General function:
    Involved in 1-aminocyclopropane-1-carboxylate synthase activity
    Specific function:
    Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.
    Gene Name:
    CCBL1
    Uniprot ID:
    Q16773
    Molecular weight:
    47874.765
    Reactions
    Se-Methylselenocysteine + 2-Oxo-4-methylthiobutanoic acid → Methylselenopyruvate + L-Methioninedetails
    General function:
    Involved in oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
    Specific function:
    Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
    Gene Name:
    MSRA
    Uniprot ID:
    Q9UJ68
    Molecular weight:
    21737.41
    Reactions
    L-Methionine + thioredoxin disulfide + Water → Methionine sulfoxide + thioredoxindetails
    References
    1. Schallreuter KU, Rubsam K, Chavan B, Zothner C, Gillbro JM, Spencer JD, Wood JM: Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus. Biochem Biophys Res Commun. 2006 Mar 31;342(1):145-52. Epub 2006 Feb 3. Pubmed: 16480945
    2. Su Z, Limberis J, Martin RL, Xu R, Kolbe K, Heinemann SH, Hoshi T, Cox BF, Gintant GA: Functional consequences of methionine oxidation of hERG potassium channels. Biochem Pharmacol. 2007 Sep 1;74(5):702-11. Epub 2007 Jun 7. Pubmed: 17624316
    3. Oien DB, Moskovitz J: Ablation of the mammalian methionine sulfoxide reductase A affects the expression level of cysteine deoxygenase. Biochem Biophys Res Commun. 2007 Jan 12;352(2):556-9. Epub 2006 Nov 20. Pubmed: 17126812
    4. Rouhier N, Vieira Dos Santos C, Tarrago L, Rey P: Plant methionine sulfoxide reductase A and B multigenic families. Photosynth Res. 2006 Sep;89(2-3):247-62. Epub 2006 Sep 22. Pubmed: 17031545
    5. Gand A, Antoine M, Boschi-Muller S, Branlant G: Characterization of the amino acids involved in substrate specificity of methionine sulfoxide reductase A. J Biol Chem. 2007 Jul 13;282(28):20484-91. Epub 2007 May 11. Pubmed: 17500063
    General function:
    Involved in zinc ion binding
    Specific function:
    Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.
    Gene Name:
    BHMT
    Uniprot ID:
    Q93088
    Molecular weight:
    44998.205
    Reactions
    Trimethylammonioacetate + Homocysteine → Dimethylglycine + L-Methioninedetails
    References
    1. Slow S, Garrow TA: Liver choline dehydrogenase and kidney betaine-homocysteine methyltransferase expression are not affected by methionine or choline intake in growing rats. J Nutr. 2006 Sep;136(9):2279-83. Pubmed: 16920841
    2. Sparks JD, Collins HL, Chirieac DV, Cianci J, Jokinen J, Sowden MP, Galloway CA, Sparks CE: Hepatic very-low-density lipoprotein and apolipoprotein B production are increased following in vivo induction of betaine-homocysteine S-methyltransferase. Biochem J. 2006 Apr 15;395(2):363-71. Pubmed: 16396637
    3. Uthus EO, Reeves PG, Saari JT: Copper deficiency decreases plasma homocysteine in rats. J Nutr. 2007 Jun;137(6):1370-4. Pubmed: 17513393
    4. Liu J, Xie Y, Cooper R, Ducharme DM, Tennant R, Diwan BA, Waalkes MP: Transplacental exposure to inorganic arsenic at a hepatocarcinogenic dose induces fetal gene expression changes in mice indicative of aberrant estrogen signaling and disrupted steroid metabolism. Toxicol Appl Pharmacol. 2007 May 1;220(3):284-91. Epub 2007 Feb 6. Pubmed: 17350061
    5. Hazra A, Wu K, Kraft P, Fuchs CS, Giovannucci EL, Hunter DJ: Twenty-four non-synonymous polymorphisms in the one-carbon metabolic pathway and risk of colorectal adenoma in the Nurses' Health Study. Carcinogenesis. 2007 Jul;28(7):1510-9. Epub 2007 Mar 26. Pubmed: 17389618
    General function:
    Involved in nucleotide binding
    Specific function:
    Not Available
    Gene Name:
    MARS
    Uniprot ID:
    P56192
    Molecular weight:
    101114.925
    Reactions
    Adenosine triphosphate + L-Methionine + tRNA(Met) → Adenosine monophosphate + Pyrophosphate + L-methionyl-tRNA(Met)details
    Adenosine triphosphate + L-Methionine + tRNA(Met) → Adenosine monophosphate + Pyrophosphate + L-Methionyl-tRNAdetails
    References
    1. Chwatko G, Boers GH, Strauss KA, Shih DM, Jakubowski H: Mutations in methylenetetrahydrofolate reductase or cystathionine beta-synthase gene, or a high-methionine diet, increase homocysteine thiolactone levels in humans and mice. FASEB J. 2007 Jun;21(8):1707-13. Epub 2007 Feb 27. Pubmed: 17327360
    2. Jakubowski H: Pathophysiological consequences of homocysteine excess. J Nutr. 2006 Jun;136(6 Suppl):1741S-1749S. Pubmed: 16702349
    3. Vaughan MD, Sampson PB, Daub E, Honek JF: Investigation of bioisosteric effects on the interaction of substrates/ inhibitors with the methionyl-tRNA synthetase from Escherichia coli. Med Chem. 2005 May;1(3):227-37. Pubmed: 16787318
    General function:
    Involved in glutamate-ammonia ligase activity
    Specific function:
    This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner (By similarity). Essential for proliferation of fetal skin fibroblasts.
    Gene Name:
    GLUL
    Uniprot ID:
    P15104
    Molecular weight:
    42064.15
    References
    1. Rowe WB, Meister A: Studies on the inhibition of glutamine synthetase by methionine sulfone. Biochemistry. 1973 Apr 10;12(8):1578-82. Pubmed: 4144717
    2. Rowe WB, Ronzio RA, Meister A: Inhibition of glutamine synthetase by methionine sulfoximine. Studies on methionine sulfoximine phosphate. Biochemistry. 1969 Jun;8(6):2674-80. Pubmed: 4308004
    3. Orr J, Haselkorn R: Regulation of glutamine synthetase activity and synthesis in free-living and symbiotic Anabaena spp. J Bacteriol. 1982 Nov;152(2):626-35. Pubmed: 6127334
    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 (By similarity).
    Gene Name:
    LIAS
    Uniprot ID:
    O43766
    Molecular weight:
    41910.695
    Reactions
    Protein N(6)-(octanoyl)lysine + Hydrogen sulfide + S-Adenosylmethionine → protein N(6)-(lipoyl)lysine + L-Methionine + 5'-Deoxyadenosinedetails
    Protein N6-(octanoyl)lysine + Sulfur donor + S-Adenosylmethionine → Protein N6-(lipoyl)lysine + L-Methionine + 5'-Deoxyadenosinedetails
    Octanoyl-[acp] + Sulfur donor + S-Adenosylmethionine → Lipoyl-[acp] + L-Methionine + 5'-Deoxyadenosinedetails
    General function:
    Involved in dTDP-4-dehydrorhamnose reductase activity
    Specific function:
    Non-catalytic regulatory subunit of S-adenosylmethionine synthetase 2 (MAT2A), an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates the activity of S-adenosylmethionine synthetase 2 by changing its kinetic properties, rendering the enzyme more susceptible to S-adenosylmethionine inhibition.
    Gene Name:
    MAT2B
    Uniprot ID:
    Q9NZL9
    Molecular weight:
    Not Available
    Reactions
    Phosphoric acid + Pyrophosphate + S-Adenosylmethionine → Adenosine triphosphate + L-Methionine + Waterdetails
    References
    1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
    2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
    3. LeGros L, Halim AB, Chamberlin ME, Geller A, Kotb M: Regulation of the human MAT2B gene encoding the regulatory beta subunit of methionine adenosyltransferase, MAT II. J Biol Chem. 2001 Jul 6;276(27):24918-24. Epub 2001 May 3. Pubmed: 11337507
    General function:
    Involved in zinc ion binding
    Specific function:
    Involved in the regulation of homocysteine metabolism. Converts homocysteine to methionine using S-methylmethionine (SMM) as a methyl donor.
    Gene Name:
    BHMT2
    Uniprot ID:
    Q9H2M3
    Molecular weight:
    33166.69
    Reactions
    Trimethylammonioacetate + Homocysteine → Dimethylglycine + L-Methioninedetails
    References
    1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
    2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
    General function:
    Involved in aminopeptidase activity
    Specific function:
    Removes the amino-terminal methionine from nascent proteins. The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo
    Gene Name:
    METAP2
    Uniprot ID:
    P50579
    Molecular weight:
    52891.1
    References
    1. Upadhya R, Zhang HS, Weiss LM: System for expression of microsporidian methionine amino peptidase type 2 (MetAP2) in the yeast Saccharomyces cerevisiae. Antimicrob Agents Chemother. 2006 Oct;50(10):3389-95. Epub 2006 Aug 17. Pubmed: 16917013
    2. Sheppard GS, Wang J, Kawai M, Fidanze SD, BaMaung NY, Erickson SA, Barnes DM, Tedrow JS, Kolaczkowski L, Vasudevan A, Park DC, Wang GT, Sanders WJ, Mantei RA, Palazzo F, Tucker-Garcia L, Lou P, Zhang Q, Park CH, Kim KH, Petros A, Olejniczak E, Nettesheim D, Hajduk P, Henkin J, Lesniewski R, Davidsen SK, Bell RL: Discovery and optimization of anthranilic acid sulfonamides as inhibitors of methionine aminopeptidase-2: a structural basis for the reduction of albumin binding. J Med Chem. 2006 Jun 29;49(13):3832-49. Pubmed: 16789740
    3. Addlagatta A, Matthews BW: Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human Type 1 methionine aminopeptidase. Protein Sci. 2006 Aug;15(8):1842-8. Epub 2006 Jul 5. Pubmed: 16823043
    4. Hu X, Addlagatta A, Lu J, Matthews BW, Liu JO: Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression. Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18148-53. Epub 2006 Nov 17. Pubmed: 17114291
    5. Nonato MC, Widom J, Clardy J: Human methionine aminopeptidase type 2 in complex with L- and D-methionine. Bioorg Med Chem Lett. 2006 May 15;16(10):2580-3. Epub 2006 Mar 15. Pubmed: 16540317
    General function:
    Involved in oxidoreductase activity
    Specific function:
    Lysosomal L-amino-acid oxidase with highest specific activity with phenylalanine. May play a role in lysosomal antigen processing and presentation (By similarity).
    Gene Name:
    IL4I1
    Uniprot ID:
    Q96RQ9
    Molecular weight:
    65327.26
    Reactions
    L-Methionine + Water + Oxygen → 2-Oxo-4-methylthiobutanoic acid + Ammonia + Hydrogen peroxidedetails
    General function:
    Involved in transferase activity, transferring nitrogenous groups
    Specific function:
    Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro) (By similarity).
    Gene Name:
    CCBL2
    Uniprot ID:
    Q6YP21
    Molecular weight:
    51399.855
    Reactions
    Se-Methylselenocysteine + 2-Oxo-4-methylthiobutanoic acid → Methylselenopyruvate + L-Methioninedetails
    General function:
    Involved in peptide-methionine-(S)-S-oxide reductase activity
    Specific function:
    Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine (By similarity). Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance.
    Gene Name:
    MSRB2
    Uniprot ID:
    Q9Y3D2
    Molecular weight:
    19536.055
    Reactions
    L-Methionine + oxidized thioredoxin → L-methionine R-oxide + reduced thioredoxindetails
    References
    1. Schallreuter KU, Rubsam K, Chavan B, Zothner C, Gillbro JM, Spencer JD, Wood JM: Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus. Biochem Biophys Res Commun. 2006 Mar 31;342(1):145-52. Epub 2006 Feb 3. Pubmed: 16480945
    2. Ranaivoson FM, Kauffmann B, Neiers F, Wu J, Boschi-Muller S, Panjikar S, Aubry A, Branlant G, Favier F: The X-ray structure of the N-terminal domain of PILB from Neisseria meningitidis reveals a thioredoxin-fold. J Mol Biol. 2006 Apr 28;358(2):443-54. Epub 2006 Feb 28. Pubmed: 16530221
    General function:
    Involved in peptide-methionine-(S)-S-oxide reductase activity
    Specific function:
    Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine. Isoform 2 is essential for hearing.
    Gene Name:
    MSRB3
    Uniprot ID:
    Q8IXL7
    Molecular weight:
    20010.23
    Reactions
    L-Methionine + oxidized thioredoxin → L-methionine R-oxide + reduced thioredoxindetails
    General function:
    Involved in nucleotide binding
    Specific function:
    Not Available
    Gene Name:
    MARS2
    Uniprot ID:
    Q96GW9
    Molecular weight:
    66590.29
    Reactions
    Adenosine triphosphate + L-Methionine + tRNA(Met) → Adenosine monophosphate + Pyrophosphate + L-methionyl-tRNA(Met)details
    Adenosine triphosphate + L-Methionine + tRNA(Met) → Adenosine monophosphate + Pyrophosphate + L-Methionyl-tRNAdetails
    References
    1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
    2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
    3. Spencer AC, Heck A, Takeuchi N, Watanabe K, Spremulli LL: Characterization of the human mitochondrial methionyl-tRNA synthetase. Biochemistry. 2004 Aug 3;43(30):9743-54. Pubmed: 15274629
    General function:
    Involved in peptide-methionine-(S)-S-oxide reductase activity
    Specific function:
    Not Available
    Gene Name:
    MSRB1
    Uniprot ID:
    Q9NZV6
    Molecular weight:
    12760.095
    Reactions
    L-Methionine + oxidized thioredoxin → L-methionine R-oxide + reduced thioredoxindetails
    References
    1. Kim HY, Gladyshev VN: Alternative first exon splicing regulates subcellular distribution of methionine sulfoxide reductases. BMC Mol Biol. 2006 Mar 16;7:11. Pubmed: 16542431
    2. Kim HY, Fomenko DE, Yoon YE, Gladyshev VN: Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases. Biochemistry. 2006 Nov 21;45(46):13697-704. Pubmed: 17105189

    Transporters

    General function:
    Involved in transmembrane transport
    Specific function:
    Sodium-independent transporter that mediates the update of aromatic acid. Can function as a net efflux pathway for aromatic amino acids in the basosolateral epithelial cells
    Gene Name:
    SLC16A10
    Uniprot ID:
    Q8TF71
    Molecular weight:
    55492.1
    References
    1. Kim DK, Kanai Y, Chairoungdua A, Matsuo H, Cha SH, Endou H: Expression cloning of a Na+-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters. J Biol Chem. 2001 May 18;276(20):17221-8. Epub 2001 Feb 20. Pubmed: 11278508