Banner
Identification
Name L-Methionine
Accession Number DB00134 (NUTR00038)
Type small molecule
Groups approved, nutraceutical
Description

A sulfur containing essential amino acid that is important in many body functions. It is a chelating agent for heavy metals. [PubChem]
Structure Thumb
Download: MOL | SDF | SMILES | InChI
Display: 2D Structure | 3D Structure
Synonyms
  • (S)-2-Amino-4-(methylthio)butanoic acid
  • 2-Amino-4-(methylthio)butyric acid
  • a-Amino-g-methylmercaptobutyric acid
  • g-Methylthio-a-aminobutyric acid
  • L-(-)-Methionine
  • L-a-Amino-g-methylthiobutyric acid
  • Methionine
Brand names
  • Acimethin
  • Cymethion
Brand name mixtures Not Available
Categories
  • Dietary supplement
  • Micronutrient
  • Essential Amino Acids
CAS number 63-68-3
Weight Average: 149.211
Monoisotopic: 149.051049291
Chemical Formula C5H11NO2S
InChI Key InChIKey=FFEARJCKVFRZRR-BYPYZUCNSA-N
InChI
InChI=1S/C5H11NO2S/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-/m0/s1
Plain Text
IUPAC Name
(2S)-2-amino-4-(methylsulfanyl)butanoic acid
SMILES
CSCC[C@H](N)C(O)=O
Plain Text
Mass Spec show (9.4 KB)
Taxonomy
Kingdom Organic
Classes
  • Amino Acids
  • Carboxylic Acids and Derivatives
Substructures
  • Amino Acids
  • Ethers
  • Hydroxy Compounds
  • Acetates
  • Aliphatic and Aryl Amines
  • Carboxylic Acids and Derivatives
Pharmacology
Indication Used for protein synthesis including the formation of SAMe, L-homocysteine, L-cysteine, taurine, and sulfate.
Pharmacodynamics L-Methionine is a principle supplier of sulfur which prevents disorders of the hair, skin and nails; helps lower cholesterol levels by increasing the liver's production of lecithin; reduces liver fat and protects the kidneys; a natural chelating agent for heavy metals; regulates the formation of ammonia and creates ammonia-free urine which reduces bladder irritation; influences hair follicles and promotes hair growth. L-methionine may protect against the toxic effects of hepatotoxins, such as acetaminophen. Methionine may have antioxidant activity.
Mechanism of action The mechanism of the possible anti-hepatotoxic activity of L-methionine is not entirely clear. It is thought that metabolism of high doses of acetaminophen in the liver lead to decreased levels of hepatic glutathione and increased oxidative stress. L-methionine is a precursor to L-cysteine. L-cysteine itself may have antioxidant activity. L-cysteine is also a precursor to the antioxidant glutathione. Antioxidant activity of L-methionine and metabolites of L-methionine appear to account for its possible anti-hepatotoxic activity. Recent research suggests that methionine itself has free-radical scavenging activity by virtue of its sulfur, as well as its chelating ability.
Absorption Absorbed from the lumen of the small intestine into the enterocytes by an active transport process.
Volume of distribution Not Available
Protein binding Not Available
Metabolism

Hepatic
Route of elimination Not Available
Half life Not Available
Clearance Not Available
Toxicity Doses of L-methionine of up to 250 mg daily are generally well tolerated. Higher doses may cause nausea, vomiting and headache. Healthy adults taking 8 grams of L-methionine daily for four days were found to have reduced serum folate levels and leucocytosis. Healthy adults taking 13.9 grams of L-methionine daily for five days were found to have changes in serum pH and potassium and increased urinary calcium excretion. Schizophrenic patients given 10 to 20 grams of L-methionine daily for two weeks developed functional psychoses. Single doses of 8 grams precipitated encephalopathy in patients with cirrhosis.
Affected organisms
  • Humans and other mammals
Pathways Not Available
Pharmacoeconomics
Manufacturers Not Available
Packagers
Dosage forms
Form Route Strength
Capsule Oral 500 mg
Powder Oral
Tablet Oral 200 mg
Tablet Oral 500 mg
Prices
Unit description Cost Unit
Dl-methionine powder 0.26 USD g
Methionine powder 0.03 USD g
Patents Not Available
Properties
State solid
Melting point 276-279 oC
Experimental Properties
Property Value Source
water solubility 56.6 mg/mL at 25 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] PhysProp
logP -1.9 PhysProp
logS -0.42 [ADME Research, USCD] PhysProp
Predicted Properties
Property Value Source
water solubility 2.39e+01 g/l ALOGPS
logP -1.85 ALOGPS
logP -2.33 ChemAxon Molconvert
logS -0.80 ALOGPS
pKa ChemAxon Molconvert
hydrogen acceptor count 3 ChemAxon Molconvert
hydrogen donor count 2 ChemAxon Molconvert
polar surface area 63.32 ChemAxon Molconvert
rotatable bond count 4 ChemAxon Molconvert
refractivity 37.59 ChemAxon Molconvert
polarizability 15.50 ChemAxon Molconvert
References
Synthesis Reference Not Available
General Reference Not Available
External Links
Resource Link
KEGG Drug D04983 Link_out
KEGG Compound C01733 Link_out
PubChem Compound 6137 Link_out
PubChem Substance 46505750 Link_out
ChemSpider 5907 Link_out
ChEBI 16811 Link_out
ChEMBL 16811 Link_out
HET MET Link_out
Drug Product Database 0 Link_out
PDRhealth http://www.pdrhealth.com/drug_info/nmdrugprofiles/nutsupdrugs/lme_0173.shtml Link_out
ATC Codes
  • V03AB26
AHFS Codes Not Available
PDB Entries
FDA label Not Available
MSDS show (72.8 KB)
Interactions
Drug Interactions
Drug Interaction
Food Interactions
  • Take with food.
Targets

1. Methionine synthase reductase, mitochondrial

Pharmacological action: unknown
Actions: product of

Involved in the reductive regeneration of cob(I)alamin cofactor required for the maintenance of methionine synthase in a functional state

Organism class: human
UniProt ID: Q9UBK8 Link_out
Gene: MTRR Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
  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
  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

2. Methionine synthase

Pharmacological action: unknown
Actions: product of
Organism class: human
UniProt ID: Q99707 Link_out
Gene: MTR Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Taurog RE, Matthews RG: Activation of methyltetrahydrofolate by cobalamin-independent methionine synthase. Biochemistry. 2006 Apr 25;45(16):5092-102. Pubmed
  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
  3. Reynolds E: Vitamin B12, folic acid, and the nervous system. Lancet Neurol. 2006 Nov;5(11):949-60. Pubmed
  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
  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

3. Methionine aminopeptidase 2

Pharmacological action: unknown
Actions: product of

Removes the amino-terminal methionine from nascent proteins

Organism class: human
UniProt ID: P50579 Link_out
Gene: METAP2 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
  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
  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
  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
  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

4. Betaine--homocysteine S-methyltransferase 1

Pharmacological action: unknown
Actions: product of

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

Organism class: human
UniProt ID: Q93088 Link_out
Gene: BHMT Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
  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
  3. Uthus EO, Reeves PG, Saari JT: Copper deficiency decreases plasma homocysteine in rats. J Nutr. 2007 Jun;137(6):1370-4. Pubmed
  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
  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

5. Betaine--homocysteine S-methyltransferase 2

Pharmacological action: unknown
Actions: product of

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

Organism class: human
UniProt ID: Q9H2M3 Link_out
Gene: BHMT2 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
  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
Enzymes

1. Glutamine synthetase

Actions: inhibitor

ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine

UniProt ID: P15104 Link_out
Gene: GLUL Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
  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
  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

2. Methylenetetrahydrofolate reductase

Actions: inhibitor

Catalyzes the conversion of 5,10- methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co- substrate for homocysteine remethylation to methionine

UniProt ID: P42898 Link_out
Gene: MTHFR Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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

3. S-adenosylmethionine synthetase isoform type-2

Actions: substrate

Catalyzes the formation of S-adenosylmethionine from methionine and ATP

UniProt ID: P31153 Link_out
Gene: MAT2A Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
  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
  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
  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

4. Methionine-R-sulfoxide reductase B2

Actions: substrate
UniProt ID: Q9Y3D2 Link_out
Gene: MSRB2 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
  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

5. S-adenosylmethionine synthetase isoform type-1

Actions: substrate

Catalyzes the formation of S-adenosylmethionine from methionine and ATP

UniProt ID: Q00266 Link_out
Gene: MAT1A Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
  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
  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
  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
  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

6. Methionine-R-sulfoxide reductase

Actions: substrate
UniProt ID: Q9NZV6 Link_out
Gene: SEPX1 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
  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

7. Peptide methionine sulfoxide reductase

Actions: substrate

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

UniProt ID: Q9UJ68 Link_out
Gene: MSRA Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
  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
  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
  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
  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

8. Methionyl-tRNA synthetase, cytoplasmic

Actions: substrate
UniProt ID: P56192 Link_out
Gene: MARS Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
  2. Jakubowski H: Pathophysiological consequences of homocysteine excess. J Nutr. 2006 Jun;136(6 Suppl):1741S-1749S. Pubmed
  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

9. Methionyl-tRNA synthetase, mitochondrial

Actions: substrate

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)

UniProt ID: Q96GW9 Link_out
Gene: MARS2 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
  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
  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

10. Methionine adenosyltransferase 2 subunit beta

Actions: substrate

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

UniProt ID: Q9NZL9 Link_out
Gene: MAT2B Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
  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
  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
Transporters

1. Monocarboxylate transporter 10

Actions: inhibitor

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 (By similarity)

UniProt ID: Q8TF71 Link_out
Gene: SLC16A10 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

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
Comments
Drug created on June 13, 2005 07:24 / Updated on July 22, 2011 11:00

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.