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Chemistry

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Also known as: L-methionine, 63-68-3, H-met-oh, (s)-2-amino-4-(methylthio)butanoic acid, Cymethion, L-(-)-methionine
Molecular Formula
C5H11NO2S
Molecular Weight
149.21  g/mol
InChI Key
FFEARJCKVFRZRR-BYPYZUCNSA-N
FDA UNII
AE28F7PNPL

L-Methionine
A sulfur-containing essential L-amino acid that is important in many body functions.
1 2D Structure

L-Methionine

2 Identification
2.1 Computed Descriptors
2.1.1 IUPAC Name
(2S)-2-amino-4-methylsulfanylbutanoic acid
2.1.2 InChI
InChI=1S/C5H11NO2S/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-/m0/s1
2.1.3 InChI Key
FFEARJCKVFRZRR-BYPYZUCNSA-N
2.1.4 Canonical SMILES
CSCCC(C(=O)O)N
2.1.5 Isomeric SMILES
CSCC[C@@H](C(=O)O)N
2.2 Other Identifiers
2.2.1 UNII
AE28F7PNPL
2.3 Synonyms
2.3.1 MeSH Synonyms

1. L-isomer Methionine

2. L-methionine

3. Liquimeth

4. Methionine, L Isomer

5. Methionine, L-isomer

6. Pedameth

2.3.2 Depositor-Supplied Synonyms

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

2.4 Create Date
2004-09-16
3 Chemical and Physical Properties
Molecular Weight 149.21 g/mol
Molecular Formula C5H11NO2S
XLogP3-1.9
Hydrogen Bond Donor Count2
Hydrogen Bond Acceptor Count4
Rotatable Bond Count4
Exact Mass149.05104977 g/mol
Monoisotopic Mass149.05104977 g/mol
Topological Polar Surface Area88.6 Ų
Heavy Atom Count9
Formal Charge0
Complexity97
Isotope Atom Count0
Defined Atom Stereocenter Count1
Undefined Atom Stereocenter Count0
Defined Bond Stereocenter Count0
Undefined Bond Stereocenter Count0
Covalently Bonded Unit Count1
4 Drug and Medication Information
4.1 Therapeutic Uses

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.


4.2 Drug Warning

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).


4.3 Drug Indication

Used for protein synthesis including the formation of SAMe, L-homocysteine, L-cysteine, taurine, and sulfate.


5 Pharmacology and Biochemistry
5.1 Pharmacology

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.


5.2 ATC Code

V - Various

V03 - All other therapeutic products

V03A - All other therapeutic products

V03AB - Antidotes

V03AB26 - Methionine


5.3 Absorption, Distribution and Excretion

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.


5.4 Metabolism/Metabolites

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.


5.5 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.


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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API | Excipient name

L-Methionine

Synonyms

63-68-3, H-met-oh, (s)-2-amino-4-(methylthio)butanoic acid, Cymethion, L-(-)-methionine, S-methionine

Cas Number

63-68-3

Unique Ingredient Identifier (UNII)

AE28F7PNPL

About L-Methionine

A sulfur-containing essential L-amino acid that is important in many body functions.

L-Methionine Manufacturers

A L-Methionine manufacturer is defined as any person or entity involved in the manufacture, preparation, processing, compounding or propagation of L-Methionine, including repackagers and relabelers. The FDA regulates L-Methionine manufacturers to ensure that their products comply with relevant laws and regulations and are safe and effective to use. L-Methionine API Manufacturers are required to adhere to Good Manufacturing Practices (GMP) to ensure that their products are consistently manufactured to meet established quality criteria.

click here to find a list of L-Methionine manufacturers with USDMF, JDMF, KDMF, CEP, GMP, COA and API Price related information on PhamaCompass.

L-Methionine Suppliers

A L-Methionine supplier is an individual or a company that provides L-Methionine active pharmaceutical ingredient (API) or L-Methionine finished formulations upon request. The L-Methionine suppliers may include L-Methionine API manufacturers, exporters, distributors and traders.

click here to find a list of L-Methionine suppliers with USDMF, JDMF, KDMF, CEP, GMP, COA and API Price related information on PharmaCompass.

L-Methionine USDMF

A L-Methionine DMF (Drug Master File) is a document detailing the whole manufacturing process of L-Methionine active pharmaceutical ingredient (API) in detail. Different forms of L-Methionine DMFs exist exist since differing nations have different regulations, such as L-Methionine USDMF, ASMF (EDMF), JDMF, CDMF, etc.

A L-Methionine DMF submitted to regulatory agencies in the US is known as a USDMF. L-Methionine USDMF includes data on L-Methionine's chemical properties, information on the facilities and procedures used, and details about packaging and storage. The L-Methionine USDMF is kept confidential to protect the manufacturer’s intellectual property.

click here to find a list of L-Methionine suppliers with USDMF on PharmaCompass.

L-Methionine JDMF

The Pharmaceuticals and Medical Devices Agency (PMDA) established the Japan Drug Master File (JDMF), also known as the Master File (MF), to permit Japanese and foreign manufacturers of drug substances, intermediates, excipients, raw materials, and packaging materials (‘Products’) to voluntarily register confidential information about the production and management of their products in Japan.

The L-Methionine Drug Master File in Japan (L-Methionine JDMF) empowers L-Methionine API manufacturers to present comprehensive information (e.g., production methods, data, etc.) to the review authority, i.e., PMDA (Pharmaceuticals & Medical Devices Agency).

PMDA reviews the L-Methionine JDMF during the approval evaluation for pharmaceutical products. At the time of L-Methionine JDMF registration, PMDA checks if the format is accurate, if the necessary items have been included (application), and if data has been attached.

click here to find a list of L-Methionine suppliers with JDMF on PharmaCompass.

L-Methionine GMP

L-Methionine Active pharmaceutical ingredient (API) is produced in GMP-certified manufacturing facility.

GMP stands for Good Manufacturing Practices, which is a system used in the pharmaceutical industry to make sure that goods are regularly produced and monitored in accordance with quality standards. The FDA’s current Good Manufacturing Practices requirements are referred to as cGMP or current GMP which indicates that the company follows the most recent GMP specifications. The World Health Organization (WHO) has its own set of GMP guidelines, called the WHO GMP. Different countries can also set their own guidelines for GMP like China (Chinese GMP) or the EU (EU GMP).

PharmaCompass offers a list of L-Methionine GMP manufacturers, exporters & distributors, which can be sorted by USDMF, JDMF, KDMF, CEP (COS), WC, API price, and more, enabling you to easily find the right L-Methionine GMP manufacturer or L-Methionine GMP API supplier for your needs.

L-Methionine CoA

A L-Methionine CoA (Certificate of Analysis) is a formal document that attests to L-Methionine's compliance with L-Methionine specifications and serves as a tool for batch-level quality control.

L-Methionine CoA mostly includes findings from lab analyses of a specific batch. For each L-Methionine CoA document that a company creates, the USFDA specifies specific requirements, such as supplier information, material identification, transportation data, evidence of conformity and signature data.

L-Methionine may be tested according to a variety of international standards, such as European Pharmacopoeia (L-Methionine EP), L-Methionine JP (Japanese Pharmacopeia) and the US Pharmacopoeia (L-Methionine USP).

Inform the supplier about your product requirements, specifying if you need a product with particular monograph like EP (Ph. Eur.), USP, JP, BP, or any other quality. In addition, clarify whether you need hydrochloride (HCl), anhydricum, base, micronisatum or a specific level of purity. To find reputable suppliers, utilize the filters and select those certified by GMP, FDA, or any other certification as per your requirement.
For your convenience, we have listed synonyms and CAS numbers to help you find the best supplier. The use of synonyms and CAS numbers can be helpful in identifying potential suppliers, but it is crucial to note that they might not always indicate the exact same product. It is important to confirm the product details with the supplier before making a purchase to ensure that it meets your requirements.
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