1. L-isomer Methionine
2. L-methionine
3. Liquimeth
4. Methionine, L Isomer
5. Methionine, L-isomer
6. Pedameth
1. L-methionine
2. 63-68-3
3. H-met-oh
4. (s)-2-amino-4-(methylthio)butanoic Acid
5. Cymethion
6. L-(-)-methionine
7. S-methionine
8. Liquimeth
9. L-methioninum
10. Methilanin
11. Neo-methidin
12. (l)-methionine
13. Methionine (van)
14. Acimethin
15. Metionina [dcit]
16. L-methionin
17. (2s)-2-amino-4-(methylsulfanyl)butanoic Acid
18. (s)-methionine
19. L-alpha-amino-gamma-methylmercaptobutyric Acid
20. H-met-h
21. Methioninum [inn-latin]
22. Metionina
23. Methioninum
24. L-homocysteine, S-methyl-
25. L(-)-amino-gamma-methylthiobutyric Acid
26. L-met
27. L-alpha-amino-gamma-methylthiobutyric Acid
28. L-gamma-methylthio-alpha-aminobutyric Acid
29. Met
30. Ccris 5528
31. Ccris 5536
32. Methionine, L-
33. Hsdb 4317
34. 2-amino-4-methylthiobutanoic Acid (s)-
35. 2-amino-4-(methylthio)butyric Acid, (s)-
36. (2s)-2-amino-4-methylsulfanyl-butanoic Acid
37. Butanoic Acid, 2-amino-4-(methylthio)-, (s)-
38. (s)-2-amino-4-(methylthio)butyric Acid
39. Toxin War (bacillus Thuringiensis Strain Ps205c)
40. (2s)-2-amino-4-methylsulfanylbutanoic Acid
41. L-a-amino-g-methylthiobutyric Acid
42. Carbon-11 Methionine
43. S-methyl-l-homocysteine
44. (s)-(+)-methionine
45. Mfcd00063097
46. Ae28f7pnpl
47. Gamma-methylthio-alpha-aminobutyric Acid
48. Chembl42336
49. Chebi:16643
50. Poly-l-methionine
51. L-2-amino-4methylthiobutyric Acid
52. Nsc-22946
53. 58576-49-1
54. Polymethionine
55. Methionine [usan:inn]
56. C-11 Methionine
57. 1006386-95-3
58. L-2-amino-4-(methylthio)butyric Acid
59. Einecs 200-562-9
60. Unii-ae28f7pnpl
61. (2s)-2-amino-4-(methylsulfanyl)butanoate
62. Nsc 22946
63. C-11 Met
64. L-2-amino-4-(methylthio)butanoic Acid
65. L-lobamine
66. 3h-l-methionine
67. G-methylthio-a-aminobutyric Acid
68. Racemic Methionine
69. 1wkm
70. D-2-amino-4-(methylthio)butanoic Acid
71. Methionine [usan:usp:inn:ban]
72. Toxin War
73. (35s)methionine
74. 2-amino-4-(methylthio)butyrate
75. Methionine (usp)
76. L(-)-methionin
77. A-amino-g-methylmercaptobutyric Acid
78. L-methionine,(s)
79. (r)-2-amino-4-(methylmercapto)butyric Acid
80. 1pg2
81. 1qq9
82. L-methionine-[34s]
83. L-methionine Z (tn)
84. Methionine [ii]
85. Methionine [mi]
86. L-methionine (jp17)
87. Methionine [inn]
88. Methionine [hsdb]
89. Methionine [inci]
90. Methionine [usan]
91. (s)-2-amino-4-(methylmercapto)butyric Acid
92. Methionine (l-methionine)
93. Methionine [vandf]
94. Methionine, L- (8ci)
95. Bmse000044
96. Bmse000915
97. L-methionine [fcc]
98. L-methionine [jan]
99. Methionine [mart.]
100. Schembl4226
101. G-methylthio-a-aminobutyrate
102. L-methionine (h-met-oh)
103. H-met-2-chlorotrityl Resin
104. Methionine [who-dd]
105. 2-amino-4-methylthiobutanoate
106. L-a-amino-g-methylthiobutyrate
107. L-methionine [usp-rs]
108. Gtpl4814
109. A-amino-g-methylmercaptobutyrate
110. Dtxsid5040548
111. Schembl15702352
112. Methionine [ep Monograph]
113. Methionine [usp Monograph]
114. Pharmakon1600-01301006
115. Alpha-amino-alpha-aminobutyric Acid
116. Gamma-methylthio-alpha-aminobutyrate
117. Hy-n0326
118. Zinc1532529
119. L-2-amino-4-methylthiobutyric Acid
120. Bdbm50142500
121. Mfcd00801344
122. Nsc760117
123. S5633
124. L-alpha-amino-gamma-methylthiobutyrate
125. L-methionine, Vetec(tm), 98.5%
126. (s)-2-amino-4-(methylthio)butanoate
127. Akos000281626
128. Akos015852512
129. L-methionine, Labeled With Carbon-11
130. Alpha-amino-gamma-methylmercaptobutyrate
131. Ccg-266196
132. Cs-w020566
133. Db00134
134. Nsc-760117
135. (s)-2-amino-4-(methylthio)-butanoate
136. Leucine Impurity B [ep Impurity]
137. Ncgc00160620-01
138. Ncgc00160620-02
139. As-10898
140. (s)-2-amino-4-(methylthio)-butanoic Acid
141. Db-029971
142. L-methionine, Bioultra, >=99.5% (nt)
143. A5456
144. Am20100552
145. M0099
146. L-methionine, Saj Special Grade, >=98.5%
147. 63m683
148. C00073
149. D00019
150. D70895
151. L(-)-amino-alpha-amino-alpha-aminobutyric Acid
152. L-methionine, Reagent Grade, >=98% (hplc)
153. M-3100
154. M02939
155. M02945
156. L-methionine, Vetec(tm) Reagent Grade, >=98%
157. A934626
158. L-methionine, Cell Culture Reagent (h-l-met-oh)
159. C6cb5837-2b49-4b25-aab0-d305dafe26eb
160. Q22124685
161. F1905-8241
162. Z1250208671
163. L-methionine, Certified Reference Material, Tracecert(r)
164. Methionine, European Pharmacopoeia (ep) Reference Standard
165. N-(2ct Resin)-l-met-oh (200-400 Mesh, > 0.3 Mmol/g)
166. L-methionine, United States Pharmacopeia (usp) Reference Standard
167. L-methionine, Pharmaceutical Secondary Standard; Certified Reference Material
168. Soft Tissue Sarcoma-associated Protein (human Clone Wo2004048938-seqid-1139)
169. L-methionine, From Non-animal Source, Meets Ep, Jp, Usp Testing Specifications, Suitable For Cell Culture, 99.0-101.0%
170. L-methionine, Pharmagrade, Ajinomoto, Ep, Jp, Usp, Manufactured Under Appropriate Gmp Controls For Pharma Or Biopharmaceutical Production, Suitable For Cell Culture
| Molecular Weight | 149.21 g/mol |
|---|---|
| Molecular Formula | C5H11NO2S |
| XLogP3 | -1.9 |
| Hydrogen Bond Donor Count | 2 |
| Hydrogen Bond Acceptor Count | 4 |
| Rotatable Bond Count | 4 |
| Exact Mass | 149.05104977 g/mol |
| Monoisotopic Mass | 149.05104977 g/mol |
| Topological Polar Surface Area | 88.6 Ų |
| Heavy Atom Count | 9 |
| Formal Charge | 0 |
| Complexity | 97 |
| Isotope Atom Count | 0 |
| Defined Atom Stereocenter Count | 1 |
| Undefined Atom Stereocenter Count | 0 |
| Defined Bond Stereocenter Count | 0 |
| Undefined Bond Stereocenter Count | 0 |
| Covalently Bonded Unit Count | 1 |
A sulfur containing essential amino acid that is important in many body functions. It is a chelating agent for heavy metals
National Library of Medicine's Medical Subject Headings online file (MeSH, 1999)
Methionine ... enhances the synthesis of glutathione and is used as an alternative to acetylcysteine in the treatment of paracetamol poisoning.
Sweetman SC (ed), Martindale: The Complete Drug Reference. London: Pharmaceutical Press (2009), p.1450.
... Many of signs of toxicity /of selenium poisoning/ can be prevented by high-protein diets, and by methionine in the presence of Vitamin E.
Doull, J., C.D. Klaassen, and M. D. Amdur (eds.). Casarett and Doull's Toxicology. 2nd ed. New York: Macmillan Publishing Co., 1980., p. 456
In Europe, oral methionine (10 g over 12 hours) is approved as an agent to restore depleted glutathione stores and prevent hepatotoxicity after large acetaminophen ingestions. N-Acetyl-L-cysteine remains the preferred antidote for acetaminophen overdose in the United States, Canada, Scotland, and most of England.
Ellenhorn, M.J. and D.G. Barceloux. Medical Toxicology - Diagnosis and Treatment of Human Poisoning. New York, NY: Elsevier Science Publishing Co., Inc. 1988., p. 80
For more Therapeutic Uses (Complete) data for (L)-Methionine (9 total), please visit the HSDB record page.
Methionine may cause nausea, vomiting, drowsiness, and irritability. It should not be used in patients with acidosis. Methionine may aggravate hepatic encephalopathy in patients with established liver damage; it should be used with caution in patients with severe liver disease.
Sweetman SC (ed), Martindale: The Complete Drug Reference. London: Pharmaceutical Press (2009), p. 1450.
Vomiting is a common adverse effect.
Ellenhorn, M.J. and D.G. Barceloux. Medical Toxicology - Diagnosis and Treatment of Human Poisoning. New York, NY: Elsevier Science Publishing Co., Inc. 1988., p. 163
Methionine ... may exacerbate hepatic encephalopathy when administered more than 10 hours postingestion.
Ellenhorn, M.J. and D.G. Barceloux. Medical Toxicology - Diagnosis and Treatment of Human Poisoning. New York, NY: Elsevier Science Publishing Co., Inc. 1988., p. 163
The death of a control subject after an oral load of methionine for a study of the possible relationship between homocysteine and Alzheimer's disease is reported. The subject developed postload plasma concentrations of methionine far beyond those reported previously in humans given the usual oral loading dose of methionine (100 mg/kg body wt). Her preload plasma metabolite values rule out known genetic diseases that might predispose one to unusually high methionine concentrations. The most likely explanation for these events is that the subject received a substantial overdose of methionine. The possibility that extremely high methionine concentrations may lead to severe cerebral effects is discussed, and it is recommended that any move to increase the sensitivity of the usual methionine loading test by increasing the dose of methionine either not be undertaken or be taken only with extreme care.
PMID:12067919 Cottington EM et al; Arterioscler Thromb Vasc Biol 22 (6): 1046-50 (2002).
When studying genetic factors in arteriosclerosis /the authors/ recorded acute complications during a standard methionine loading test (with a dose of 100 mg/kg bw) and assessed a 30-day mortality in a group of 296 patients with coronary artery or peripheral arterial disease and in 591 controls. Acute complications were observed in 33% of the women and 16.5% of the men. For each sex, the patients and controls exhibited the same proportion of complications. The most common symptom, dizziness, was attributable to methionine loading. In addition, isolated sleepiness, nausea, polyuria and decreased or increased blood pressure were observed in part of the subjects. None of the 887 individuals died within the 30-day period following the test...
PMID:12056788 Krupkova-Meixerova L et al; Clin Nutr 21 (2): 151-6 (2002).
Used for protein synthesis including the formation of SAMe, L-homocysteine, L-cysteine, taurine, and sulfate.
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.
V - Various
V03 - All other therapeutic products
V03A - All other therapeutic products
V03AB - Antidotes
V03AB26 - Methionine
Absorption
Absorbed from the lumen of the small intestine into the enterocytes by an active transport process.
... Rats were fed diets containing [(14)C-methyl]l-methionine ... with 6% of sodium formate, and conversion of (14)C into [(14)C]formate was measured in urine and exhaled air (as (14)CO2) ... Total oxidation of [(14)C-methyl] into CO2, amounted to 60-87% for methionine ...
The Chemical Society. Foreign Compound Metabolism in Mammals. Volume 5: A Review of the Literature Published during 1976 and 1977. London: The Chemical Society, 1979., p. 435
Although the free amino acids dissolved in the body fluids are only a very small proportion of the body's total mass of amino acids, they are very important for the nutritional and metabolic control of the body's proteins. ... Although the plasma compartment is most easily sampled, the concentration of most amino acids is higher in tissue intracellular pools. Typically, large neutral amino acids, such as leucine and phenylalanine, are essentially in equilibrium with the plasma. Others, notably glutamine, glutamic acid, and glycine, are 10- to 50-fold more concentrated in the intracellular pool. Dietary variations or pathological conditions can result in substantial changes in the concentrations of the individual free amino acids in both the plasma and tissue pools. /Amino acids/
NAS, Food and Nutrition Board, Institute of Medicine; Dietary Reference Intakes for Energy, Carbohydrate, Fiber, Fat, Fatty Acids, Cholesterol, Protein, and Amino Acids (Macronutrients). National Academy Press, Washington, D.C., pg. 596, 2009. Available from, as of March 10, 2010: https://www.nap.edu/catalog/10490.html
After ingestion, proteins are denatured by the acid in the stomach, where they are also cleaved into smaller peptides by the enzyme pepsin, which is activated by the increase in stomach acidity that occurs on feeding. The proteins and peptides then pass into the small intestine, where the peptide bonds are hydrolyzed by a variety of enzymes. These bond-specific enzymes originate in the pancreas and include trypsin, chymotrypsins, elastase, and carboxypeptidases. The resultant mixture of free amino acids and small peptides is then transported into the mucosal cells by a number of carrier systems for specific amino acids and for di- and tri-peptides, each specific for a limited range of peptide substrates. After intracellular hydrolysis of the absorbed peptides, the free amino acids are then secreted into the portal blood by other specific carrier systems in the mucosal cell or are further metabolized within the cell itself. Absorbed amino acids pass into the liver, where a portion of the amino acids are taken up and used; the remainder pass through into the systemic circulation and are utilized by the peripheral tissues. /Amino acids/
NAS, Food and Nutrition Board, Institute of Medicine; Dietary Reference Intakes for Energy, Carbohydrate, Fiber, Fat, Fatty Acids, Cholesterol, Protein, and Amino Acids (Macronutrients). National Academy Press, Washington, D.C., pg. 599, 2009. Available from, as of March 10, 2010: https://www.nap.edu/catalog/10490.html
Protein secretion into the intestine continues even under conditions of protein-free feeding, and fecal nitrogen losses (ie, nitrogen lost as bacteria in the feces) may account for 25% of the obligatory loss of nitrogen. Under this dietary circumstance, the amino acids secreted into the intestine as components of proteolytic enzymes and from sloughed mucosal cells are the only sources of amino acids for the maintenance of the intestinal bacterial biomass. ... Other routes of loss of intact amino acids are via the urine and through skin and hair loss. These losses are small by comparison with those described above, but nonetheless may have a significant impact on estimates of requirements, especially in disease states. /Amino acids/
NAS, Food and Nutrition Board, Institute of Medicine; Dietary Reference Intakes for Energy, Carbohydrate, Fiber, Fat, Fatty Acids, Cholesterol, Protein, and Amino Acids (Macronutrients). National Academy Press, Washington, D.C., pg. 600-601, 2009. Available from, as of March 10, 2010: https://www.nap.edu/catalog/10490.html
For more Absorption, Distribution and Excretion (Complete) data for (L)-Methionine (11 total), please visit the HSDB record page.
Hepatic
Product of oxidative deamination or transamination--alpha-keto-gamma-methiolbutyric acid. /From table/
Furia, T.E. (ed.). CRC Handbook of Food Additives. 2nd ed. Cleveland: The Chemical Rubber Co., 1972., p. 831
... Oxidation of methionine (S-methyl-l-cysteine and sarcosine) methyl group in vivo proceeds primarily by way of free formate, and that conversion to formate is probably not catalysed by tetrahydrofolic acid.
The Chemical Society. Foreign Compound Metabolism in Mammals. Volume 5: A Review of the Literature Published during 1976 and 1977. London: The Chemical Society, 1979., p. 435
... Methionine ... is catabolized to a large extent independently of initial activation to S-adenosyl-l-methionine. The system for catabolism ... appears analogous to one that catalyses oxidation of S-methyl-l-cysteine methyl group ... The methyl group of methionine ... /has been/ shown ... to yield formate in vitro and in vivo.
The Chemical Society. Foreign Compound Metabolism in Mammals. Volume 5: A Review of the Literature Published during 1976 and 1977. London: The Chemical Society, 1979., p. 435
Infants more rapidly metabolized methionine than adults.
NAS, Food and Nutrition Board, Institute of Medicine; Dietary Reference Intakes for Energy, Carbohydrate, Fiber, Fat, Fatty Acids, Cholesterol, Protein, and Amino Acids (Macronutrients). National Academy Press, Washington, D.C., pg. 726, 2009. Available from, as of March 10, 2010: https://www.nap.edu/catalog/10490.html
For more Metabolism/Metabolites (Complete) data for (L)-Methionine (7 total), please visit the HSDB record page.
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.
Amino acids are selected for protein synthesis by binding with transfer RNA (tRNA) in the cell cytoplasm. The information on the amino acid sequence of each individual protein is contained in the sequence of nucleotides in the messenger RNA (mRNA) molecules, which are synthesized in the nucleus from regions of DNA by the process of transcription. The mRNA molecules then interact with various tRNA molecules attached to specific amino acids in the cytoplasm to synthesize the specific protein by linking together individual amino acids; this process, known as translation, is regulated by amino acids (e.g., leucine), and hormones. Which specific proteins are expressed in any particular cell and the relative rates at which the different cellular proteins are synthesized, are determined by the relative abundances of the different mRNAs and the availability of specific tRNA-amino acid combinations, and hence by the rate of transcription and the stability of the messages. From a nutritional and metabolic point of view, it is important to recognize that protein synthesis is a continuing process that takes place in most cells of the body. In a steady state, when neither net growth nor protein loss is occurring, protein synthesis is balanced by an equal amount of protein degradation. The major consequence of inadequate protein intakes, or diets low or lacking in specific indispensable amino acids relative to other amino acids (often termed limiting amino acids), is a shift in this balance so that rates of synthesis of some body proteins decrease while protein degradation continues, thus providing an endogenous source of those amino acids most in need. /Protein synthesis/
NAS, Food and Nutrition Board, Institute of Medicine; Dietary Reference Intakes for Energy, Carbohydrate, Fiber, Fat, Fatty Acids, Cholesterol, Protein, and Amino Acids (Macronutrients). National Academy Press, Washington, D.C., pg. 601-602, 2009. Available from, as of March 10, 2010: https://www.nap.edu/catalog/10490.html
The mechanism of intracellular protein degradation, by which protein is hydrolyzed to free amino acids, is more complex and is not as well characterized at the mechanistic level as that of synthesis. A wide variety of different enzymes that are capable of splitting peptide bonds are present in cells. However, the bulk of cellular proteolysis seems to be shared between two multienzyme systems: the lysosomal and proteasomal systems. The lysosome is a membrane-enclosed vesicle inside the cell that contains a variety of proteolytic enzymes and operates mostly at acid pH. Volumes of the cytoplasm are engulfed (autophagy) and are then subjected to the action of the protease enzymes at high concentration. This system is thought to be relatively unselective in most cases, although it can also degrade specific intracellular proteins. The system is highly regulated by hormones such as insulin and glucocorticoids, and by amino acids. The second system is the ATP-dependent ubiquitin-proteasome system, which is present in the cytoplasm. The first step is to join molecules of ubiquitin, a basic 76-amino acid peptide, to lysine residues in the target protein. Several enzymes are involved in this process, which selectively targets proteins for degradation by a second component, the proteasome. /Protein degradation/
NAS, Food and Nutrition Board, Institute of Medicine; Dietary Reference Intakes for Energy, Carbohydrate, Fiber, Fat, Fatty Acids, Cholesterol, Protein, and Amino Acids (Macronutrients). National Academy Press, Washington, D.C., pg. 602, 2009. Available from, as of March 10, 2010: https://www.nap.edu/catalog/10490.html
Methionine dependence, the inability of cells to grow when the amino acid methionine is replaced in culture medium by its metabolic precursor homocysteine, is characteristic of many cancer cell lines and some tumors in situ. Most cell lines proliferate normally under these conditions. The methionine dependent tumorigenic human melanoma cell line MeWo-LC1 was derived from the methionine independent non-tumorigenic line, MeWo. MeWo-LC1 has a cellular phenotype identical to that of cells from patients with the cblC inborn error of cobalamin metabolism, with decreased synthesis of cobalamin coenzymes and decreased activity of the cobalamin-dependent enzymes methionine synthase and methylmalonylCoA mutase. Inability of cblC cells to complement the defect in MeWo-LC1 suggested that it was caused by decreased activity of the MMACHC gene. However, no potentially disease causing mutations were detected in the coding sequence of MMACHC in MeWo-LC1. No MMACHC expression was detected in MeWo-LC1 by quantitative or non-quantitative PCR. There was virtually complete methylation of a CpG island at the 5'-end of the MMACHC gene in MeWo-LC1, consistent with inactivation of the gene by methylation. The CpG island was partially methylated (30-45%) in MeWo and only lightly methylated (2-11%) in control fibroblasts. Infection of MeWo-LC1 with wild type MMACHC resulted in correction of the defect in cobalamin metabolism and restoration of the ability of cells to grow in medium containing homocysteine. /It was concluded/ that epigenetic inactivation of the MMACHC gene is responsible for methionine dependence in MeWo-LC1.
Loewy AD et al; Mol Genet Metab 96 (4): 261-7 (2009). Available from, as of March 17, 2010: https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=19200761
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