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Chemistry

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Also known as: L-tryptophan, 73-22-3, L-tryptophane, H-trp-oh, (s)-tryptophan, Tryptophane
Molecular Formula
C11H12N2O2
Molecular Weight
204.22  g/mol
InChI Key
QIVBCDIJIAJPQS-VIFPVBQESA-N
FDA UNII
8DUH1N11BX

Tryptophan
An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.
1 2D Structure

Tryptophan

2 Identification
2.1 Computed Descriptors
2.1.1 IUPAC Name
(2S)-2-amino-3-(1H-indol-3-yl)propanoic acid
2.1.2 InChI
InChI=1S/C11H12N2O2/c12-9(11(14)15)5-7-6-13-10-4-2-1-3-8(7)10/h1-4,6,9,13H,5,12H2,(H,14,15)/t9-/m0/s1
2.1.3 InChI Key
QIVBCDIJIAJPQS-VIFPVBQESA-N
2.1.4 Canonical SMILES
C1=CC=C2C(=C1)C(=CN2)CC(C(=O)O)N
2.1.5 Isomeric SMILES
C1=CC=C2C(=C1)C(=CN2)C[C@@H](C(=O)O)N
2.2 Other Identifiers
2.2.1 UNII
8DUH1N11BX
2.3 Synonyms
2.3.1 MeSH Synonyms

1. Ardeydorm

2. Ardeytropin

3. L Tryptophan

4. L Tryptophan Ratiopharm

5. L-tryptophan

6. L-tryptophan-ratiopharm

7. Levotryptophan

8. Lyphan

9. Naturruhe

10. Optimax

11. Pms Tryptophan

12. Pms-tryptophan

13. Ratio Tryptophan

14. Ratio-tryptophan

15. Trofan

16. Tryptacin

17. Tryptan

18. Tryptophan Metabolism Alterations

2.3.2 Depositor-Supplied Synonyms

1. L-tryptophan

2. 73-22-3

3. L-tryptophane

4. H-trp-oh

5. (s)-tryptophan

6. Tryptophane

7. Trofan

8. Tryptacin

9. Optimax

10. Ardeytropin

11. (2s)-2-amino-3-(1h-indol-3-yl)propanoic Acid

12. Pacitron

13. Indole-3-alanine

14. Kalma

15. L-beta-3-indolylalanine

16. L-tryptofan

17. L-trp

18. L-(-)-tryptophan

19. 3-indol-3-ylalanine

20. Tryptan

21. Lyphan

22. Tryptophan (van)

23. 1-beta-3-indolylalanine

24. Tryptophan (h-3)

25. Triptofano [spanish]

26. Tryptophanum [latin]

27. 1h-indole-3-alanine

28. Tryptophan, L-

29. 1beta-3-indolylalanine

30. (-)-tryptophan

31. 2-amino-3-indolylpropanoic Acid

32. L(-)-tryptophan

33. Triptofano

34. Tryptophanum

35. (s)-alpha-amino-1h-indole-3-propanoic Acid

36. Tryptophane [french]

37. (l)-tryptophan

38. Alpha'-amino-3-indolepropionic Acid

39. Tryptophan [usan:inn]

40. L-alpha-amino-3-indolepropionic Acid

41. L-alpha-aminoindole-3-propionic Acid

42. Sedanoct

43. (s)-alpha-aminoindole-3-propionic Acid

44. 1h-indole-3-alanine (van)

45. Eh 121

46. Trp

47. Alanine, 3-indol-3-yl-

48. Ccris 617

49. L-alanine, 3-(1h-indol-3-yl)-

50. 1h-indole-3-alanine, (s)-

51. Alpha-amino-3-indolepropionic Acid, L-

52. Hsdb 4142

53. Trytophan-

54. (s)-alpha-amino-beta-(3-indolyl)-propionic Acid

55. Nci-c01729

56. Ai3-18478

57. (s)-2-amino-3-(3-indolyl)propionic Acid

58. Indole-3-propionic Acid, Alpha-amino-

59. 1h-indole-3-propanoic Acid, Alpha-amino-, (s)-

60. Propionic Acid, 2-amino-3-indol-3-yl-

61. Chebi:16828

62. Lopac-t-0254

63. Tryptophan ((-),l,s)

64. 8duh1n11bx

65. (s)-alpha-amino-beta-indolepropionic Acid

66. Chembl54976

67. (s)-2-amino-3-(1h-indol-3-yl)propanoic Acid

68. Nsc-13119

69. Mfcd00064340

70. Dsstox_cid_1419

71. Dsstox_rid_76152

72. Dsstox_gsid_21419

73. 80206-30-0

74. L-b-3-indolylalanine

75. L-tryptophan-13c11,15n2

76. D-trp-oh

77. Cas-73-22-3

78. Propionic Acid, 2-amino-3-indol-3-yl

79. L-tryptophan (9ci)

80. Tryptophan (usp/inn)

81. (s)-a-amino-b-indolepropionic Acid

82. (s)-a-aminoindole-3-propionic Acid

83. Alanine, 3-indol-3-yl

84. Einecs 200-795-6

85. Nsc 13119

86. Unii-8duh1n11bx

87. (2s)-2-amino-3-(1h-indol-3-yl)propanoate

88. Trytophan

89. (s)-a-amino-1h-indole-3-propanoic Acid

90. Trp-01

91. L-trytophan

92. 1qaw

93. L-tryptophan,(s)

94. L-trp-oh

95. 2a4m

96. H-l-trp-oh

97. Tryptophan [ii]

98. Tryptophan [mi]

99. L-tryptophan (jp17)

100. Tryptophan [inn]

101. S(-)-1-alpha-aminoindole-3-propionic Acid

102. Tryptophan [hsdb]

103. Tryptophan [inci]

104. Tryptophan [usan]

105. Tryptophan (l-tryptophan)

106. Tryptophan [vandf]

107. Tryptophan, L- (8ci)

108. Bmse000050

109. Bmse000868

110. Bmse001017

111. Epitope Id:136043

112. Ec 200-795-6

113. T 0254

114. L-tryptophan [fcc]

115. L-tryptophan [jan]

116. Schembl7328

117. Tryptophan [mart.]

118. 2-amino-3-indolylpropanoate

119. (s)-(-)-2-amino-3-(3-indolyl)propionic Acid

120. (s)-1h-indole-3-alanine

121. Lopac0_001183

122. Gtpl717

123. L-tryptophan [vandf]

124. Mls001056750

125. Divk1c_000457

126. L-tryptophan [usp-rs]

127. (s)-a-amino-b-indolepropionate

128. 151a3008-4cfe-40c9-ac0b-467ef0cb50ea

129. Dtxsid5021419

130. (s)-a-aminoindole-3-propionate

131. Bdbm21974

132. Hms501g19

133. Kbio1_000457

134. Zinc83315

135. Tryptophan [ep Monograph]

136. 3-(1h-indol-3-yl)-l-alanine

137. L-a-amino-3-indolepropionic Acid

138. Ninds_000457

139. Alpha-aminoindole-3-propionic Acid

140. Hms3263n07

141. Pharmakon1600-01500600

142. Tryptophan [usp Monograph]

143. Tryptophan, L- [who-dd]

144. Act08662

145. Hy-n0623

146. Str02722

147. (s)-alpha-aminoindole-3-propionate

148. Tox21_201246

149. Tox21_300359

150. Tox21_501183

151. Nsc757373

152. S3987

153. (s)-alpha-amino-beta-indolepropionate

154. L-tryptophan, Vetec(tm), 98.5%

155. (s)-a-amino-1h-indole-3-propanoate

156. Akos015854052

157. Indoe-3-propionic Acid, Alpha-amino-

158. Am82273

159. Ccg-205257

160. Cs-w020011

161. Db00150

162. Lp01183

163. Nsc-757373

164. Sdccgsbi-0051150.p002

165. Idi1_000457

166. Ncgc00015994-01

167. Ncgc00094437-01

168. Ncgc00094437-02

169. Ncgc00094437-03

170. Ncgc00094437-04

171. Ncgc00094437-08

172. Ncgc00254424-01

173. Ncgc00258798-01

174. Ncgc00261868-01

175. (s)-alpha-amino-1h-indole-3-propanoate

176. Ac-17050

177. Bp-13286

178. Smr000326686

179. Ts-04426

180. Db-029986

181. L-tryptophan, Bioultra, >=99.5% (nt)

182. A7403

183. Eu-0101183

184. T0541

185. (s)-tryptophan 1h-indole-3-alanine, (s)-

186. 73t223

187. C00078

188. D00020

189. L-.alpha.-amino-3-indolepropionic Acid

190. L-tryptophan, Reagent Grade, >=98% (hplc)

191. M02943

192. P16427

193. Ab00373874_05

194. L-tryptophan, Vetec(tm) Reagent Grade, >=98%

195. (s)-2-amino-3-(1h-indol-3-yl)-propionic Acid

196. A837752

197. L-tryptophan, Cell Culture Reagent (h-l-trp-oh)

198. Q181003

199. Sr-01000075590

200. 4-(3-methoxyanilino)-4-oxobut-2-enoicacid

201. N-acetyltryptophan Impurity A [ep Impurity]

202. Sr-01000075590-1

203. F0001-2364

204. Z1245635763

205. 1h-indole-3-propanoic Acid, .alpha.-amino-, (s)-

206. L-tryptophan, Certified Reference Material, Tracecert(r)

207. Tryptophan, European Pharmacopoeia (ep) Reference Standard

208. L-tryptophan, United States Pharmacopeia (usp) Reference Standard

209. L-tryptophan, From Non-animal Source, Meets Ep, Jp, Usp Testing Specifications, Suitable For Cell Culture, 99.0-101.0%

210. L-tryptophan, 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 204.22 g/mol
Molecular Formula C11H12N2O2
XLogP3-1.1
Hydrogen Bond Donor Count3
Hydrogen Bond Acceptor Count3
Rotatable Bond Count3
Exact Mass204.089877630 g/mol
Monoisotopic Mass204.089877630 g/mol
Topological Polar Surface Area79.1 Ų
Heavy Atom Count15
Formal Charge0
Complexity245
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

Tryptophan is a precursor of serotonin. Because CNS depletion of serotonin is considered to be involved in depression, tryptophan has been used in its treatment. Although it has been given alone, evidence of effectiveness is scant and tryptophan has generally been used as adjunctive therapy in depression. It has sometimes been given with pyridoxine and ascorbic acid, which are involved in its metabolism to serotonin

Sweetman SC (ed), Martindale: The Complete Drug Reference. London: Pharmaceutical Press (2009), p.427.


/EXPTL USE/: Inhibition of Walker 256 intramuscular carcinoma in rats by admin of l-tryptophan.

PMID:5446186 Gold J; Oncology 24 (4): 291-303 (1970)


(L)-Tryptophan decreases sleep latency and slightly increases sleeping time without altering qualitative characteristics of polygraphic patterns during sleep in normal subjects. In insomniac patients, it increases sleeping time and decreases both sleep latency and number of awakenings.

PMID:4935665 Hartmann E et al; Psychopharmacologia 19 (2): 114 (1971)


Beneficial effects were observed when L-tryptophan was administered to 2 patients with myoclonus. In each case suspension of methylcellulose and water containing 1 g of (L)-tryptophan/15 mL was prepared and administered orally at a level of 10 g daily in 5 divided doses.

Delean J, Richardson JC; Lancet 2 (7940): 870-1 (1975)


For more Therapeutic Uses (Complete) data for (L)-Tryptophan (11 total), please visit the HSDB record page.


4.2 Drug Warning

Since serotonin plays a role in inducing and maintaining sleep, l-tryptophan has been administered orally to increase brain levels of serotonin. Although a dose of 1 g significantly decreased sleep latency and total time awake without altering sleep patterns, the hypnotic action is observed only during the early part of the sleep cycle, is unpredictable, and is not characterized by a satisfactory dose-response relationship. Because the hypnotic action has not been confirmed in other studies, this use of l-tryptophan must be considered investigational and the drug is not recommended in routine clinical practice. In order to avoid central serotonergic toxicity, tryptophan should not be used in patients also receiving a monoamine oxidase inhibitor or the serotonin uptake inhibitor, fluoxetine (Prozac).

American Medical Association. AMA Drug Evaluations Annual 1991. Chicago, IL: American Medical Association, 1991., p. 215


Tryptophan-containing products have been associated with the eosinophilia-myalgia syndrome. Other adverse effects that have been reported include nausea, headache, lightheadedness, and drowsiness.

Sweetman SC (ed), Martindale: The Complete Drug Reference. London: Pharmaceutical Press (2009), p.427.


An increased incidence of bladder tumours has been reported in mice given l-tryptophan orally as well as in cholesterol pellets embedded in the bladder lumen. However, there was no increase in tumour incidence when only high-dose, oral tryptophan was given.

Sweetman SC (ed), Martindale: The Complete Drug Reference. London: Pharmaceutical Press (2009), p.427.


Tryptophan has been associated with eosinophilia-myalgia syndrome; caution is advised in patients receiving the drug who develop some, but not all, of the symptoms of this syndrome. It should not be used in those with a history of eosinophilia-myalgia syndrome associated with tryptophan treatment.

Sweetman SC (ed), Martindale: The Complete Drug Reference. London: Pharmaceutical Press (2009), p.427.


For more Drug Warnings (Complete) data for (L)-Tryptophan (7 total), please visit the HSDB record page.


4.3 Drug Indication

Tryptophan may be useful in increasing serotonin production, promoting healthy sleep, managing depression by enhancing mental and emotional well-being, managing pain tolerance, and managing weight.


5 Pharmacology and Biochemistry
5.1 Pharmacology

Tryptophan is critical for the production of the body's proteins, enzymes and muscle tissue. It is also essential for the production of niacin, the synthesis of the neurotransmitter serotonin and melatonin. Tryptophan supplements can be used as natural relaxants to help relieve insomnia. Tryptophan can also reduce anxiety and depression and has been shown to reduce the intensity of migraine headaches. Other promising indications include the relief of chronic pain, reduction of impulsivity or mania and the treatment of obsessive or compulsive disorders. Tryptophan also appears to help the immune system and can reduce the risk of cardiac spasms. Tryptophan deficiencies may lead to coronary artery spasms. Tryptophan is used as an essential nutrient in infant formulas and intravenous feeding. Tryptophan is marketed as a prescription drug (Tryptan) for those who do not seem to respond well to conventional antidepressants. It may also be used to treat those afflicted with seasonal affective disorder (a winter-onset depression). Tryptopan serves as the precursor for the synthesis of serotonin (5-hydroxytryptamine, 5-HT) and melatonin (N-acetyl-5-methoxytryptamine).


5.2 MeSH Pharmacological Classification

Antidepressive Agents, Second-Generation

A structurally and mechanistically diverse group of drugs that are not tricyclics or monoamine oxidase inhibitors. The most clinically important appear to act selectively on serotonergic systems, especially by inhibiting serotonin reuptake. (See all compounds classified as Antidepressive Agents, Second-Generation.)


5.3 ATC Code

N - Nervous system

N06 - Psychoanaleptics

N06A - Antidepressants

N06AX - Other antidepressants

N06AX02 - Tryptophan


5.4 Absorption, Distribution and Excretion

(L)-Tryptophan with plant oils in soft gelatin capsules permitted lower dosage than with usual dosage form. Max of free tryptophan in serum was achieved in 1st hr whereas 4-5 times as much would be required with tablets or hard gelatin capsules.

Klosa J; Ger Offen Patent NO 2824362 12/13/79


Absorption and Fate. Tryptophan is readily absorbed from the gastro-intestinal tract. Tryptophan is extensively bound to serum albumin. It is metabolized to serotonin and other metabolites, incl kynurenine derivatives, and excreted in the urine. Pyridoxine and ascorbic acid appear to be concerned in its metabolism.

Reynolds, J.E.F., Prasad, A.B. (eds.) Martindale-The Extra Pharmacopoeia. 28th ed. London: The Pharmaceutical Press, 1982., p. 61


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


For more Absorption, Distribution and Excretion (Complete) data for (L)-Tryptophan (9 total), please visit the HSDB record page.


5.5 Metabolism/Metabolites

Hepatic.


In Hartnup disease ... tryptophane appear/s/ in urine due to defective renal and intestinal absorption of tryptophane ... It is an intermediary metabolite in the synthesis of serotonin (5-hydroxytryptamine) and 5-hydroxyindole acetic acid (HIAA).

Osol, A. and J.E. Hoover, et al. (eds.). Remington's Pharmaceutical Sciences. 15th ed. Easton, Pennsylvania: Mack Publishing Co., 1975., p. 590


Patients with bladder cancer excreted significantly more kynurenic acid, acetylkynurenine, kynurenine, and 3-hydroxykynurenine after ingesting a loading dose of L-tryptophan than did control subjects with no known disease.

Searle, C. E. (ed.). Chemical Carcinogens. ACS Monograph 173. Washington, DC: American Chemical Society, 1976., p. 443


Tryptophan is metabolized in the liver by tryptophan pyrrolase and tryptophan hydroxylase. Metabolites include hydroxytryptophan, which is then converted to serotonin, and kynurenine derivatives. Some tryptophan is converted to nicotinic acid and nicotinamide. Pyridoxine and ascorbic acid are cofactors in the decarboxylation and hydroxylation, respectively, of tryptophan; pyridoxine apparently prevents the accumulation of the kynurenine metabolites.

Sweetman SC (ed), Martindale: The Complete Drug Reference. London: Pharmaceutical Press (2009), p.427.


Yields indole-3-pyruvic acid in man ... and in rats; yields tryptamine in guinea pigs. /From table/

Goodwin, B.L. Handbook of Intermediary Metabolism of Aromatic Compounds. New York: Wiley, 1976., p. T-38


For more Metabolism/Metabolites (Complete) data for (L)-Tryptophan (21 total), please visit the HSDB record page.


5.6 Biological Half-Life

The biological half-life of tryptophan was reported to be 15.8 hr.

Reynolds, J.E.F., Prasad, A.B. (eds.) Martindale-The Extra Pharmacopoeia. 28th ed. London: The Pharmaceutical Press, 1982., p. 61


5.7 Mechanism of Action

A number of important side reactions occur during the catabolism of tryptophan on the pathway to acetoacetate. The first enzyme of the catabolic pathway is an iron porphyrin oxygenase that opens the indole ring. The latter enzyme is highly inducible, its concentration rising almost 10-fold on a diet high in tryptophan. Kynurenine is the first key branch point intermediate in the pathway. Kynurenine undergoes deamniation in a standard transamination reaction yielding kynurenic acid. Kynurenic acid and metabolites have been shown to act as antiexcitotoxics and anticonvulsives. A second side branch reaction produces anthranilic acid plus alanine. Another equivalent of alanine is produced further along the main catabolic pathway, and it is the production of these alanine residues that allows tryptophan to be classified among the glucogenic and ketogenic amino acids. The second important branch point converts kynurenine into 2-amino-3-carboxymuconic semialdehyde, which has two fates. The main flow of carbon elements from this intermediate is to glutarate. An important side reaction in liver is a transamination and several rearrangements to produce limited amounts of nicotinic acid, which leads to production of a small amount of NAD+ and NADP+.


Findings indicate that enhanced rates of serotonin turnover produced by (L)-tryptophan and physical restraint are associated with inhibition of thyroid-stimulating hormone (TSH) and stimulation of prolactin release from anterior pituitary in rats.

PMID:1083471 Mueller GP et al; Life Sci 18 (7): 715-24 (1976)


L-Tryptophan, an indispensable amino acid, serves as a precursor for several small molecules of functional significance including the vitamin niacin, the neurotransmitter serotonin, the metabolite tryptamine, and the pineal hormone melatonin. Increases in tryptophan have been shown to increase synthesis of the neurotransmitters in brain, blood, and other body organs.

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. 731, 2009. Available from, as of March 10, 2010: https://www.nap.edu/catalog/10490.html


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. /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. 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.

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


For more Mechanism of Action (Complete) data for (L)-Tryptophan (7 total), please visit the HSDB record page.


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ABOUT THIS PAGE

Looking for 73-22-3 / Tryptophan API manufacturers, exporters & distributors?

Tryptophan manufacturers, exporters & distributors 1

11

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

Send us enquiries for free, and we will assist you in establishing a direct connection with your preferred Tryptophan manufacturer or Tryptophan supplier.

PharmaCompass also assists you with knowing the Tryptophan API Price utilized in the formulation of products. Tryptophan API Price is not always fixed or binding as the Tryptophan Price is obtained through a variety of data sources. The Tryptophan Price can also vary due to multiple factors, including market conditions, regulatory modifications, or negotiated pricing deals.

API | Excipient name

Tryptophan

Synonyms

L-tryptophan, 73-22-3, L-tryptophane, H-trp-oh, (s)-tryptophan, Tryptophane

Cas Number

73-22-3

Unique Ingredient Identifier (UNII)

8DUH1N11BX

About Tryptophan

An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.

trp Manufacturers

A trp manufacturer is defined as any person or entity involved in the manufacture, preparation, processing, compounding or propagation of trp, including repackagers and relabelers. The FDA regulates trp manufacturers to ensure that their products comply with relevant laws and regulations and are safe and effective to use. trp 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 trp manufacturers with USDMF, JDMF, KDMF, CEP, GMP, COA and API Price related information on PhamaCompass.

trp Suppliers

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

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

trp USDMF

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

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

click here to find a list of trp suppliers with USDMF on PharmaCompass.

trp 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 trp Drug Master File in Japan (trp JDMF) empowers trp 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 trp JDMF during the approval evaluation for pharmaceutical products. At the time of trp 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 trp suppliers with JDMF on PharmaCompass.

trp CEP

A trp CEP of the European Pharmacopoeia monograph is often referred to as a trp Certificate of Suitability (COS). The purpose of a trp CEP is to show that the European Pharmacopoeia monograph adequately controls the purity of trp EP produced by a given manufacturer. Suppliers of raw materials can prove the suitability of trp to their clients by showing that a trp CEP has been issued for it. The manufacturer submits a trp CEP (COS) as part of the market authorization procedure, and it takes on the role of a trp CEP holder for the record. Additionally, the data presented in the trp CEP (COS) is managed confidentially and offers a centralized system acknowledged by numerous nations, exactly like the trp DMF.

A trp CEP (COS) is recognised by all 36 nations that make up the European Pharmacopoeia Convention. trp CEPs may be accepted in nations that are not members of the Ph. Eur. at the discretion of the authorities there.

click here to find a list of trp suppliers with CEP (COS) on PharmaCompass.

trp NDC

National Drug Code is a comprehensive database maintained by the FDA that contains information on all drugs marketed in the US. This directory includes information about finished drug products, unfinished drug products, and compounded drug products, including those containing trp as an active pharmaceutical ingredient (API).

Finished drug products

The FDA updates the NDC directory daily. The NDC numbers for trp API and other APIs are published in this directory by the FDA.

Unfinished drugs

The NDC unfinished drugs database includes product listing information submitted for all unfinished drugs, such as active pharmaceutical ingredients (APIs), drugs intended for further processing and bulk drug substances for compounding.

Pharmaceutical companies that manufacture trp as an active pharmaceutical ingredient (API) must furnish the FDA with an updated record of all drugs that they produce, prepare, propagate, compound, or process for commercial distribution in the US at their facilities.

Compounded drug products

The NDC directory also contains data on finished compounded human drug products that contain trp and are produced by outsourcing facilities. While these outsourcing facilities are not mandated to assign a trp NDC to their finished compounded human drug products, they may choose to do so.

click here to find a list of trp suppliers with NDC on PharmaCompass.

trp GMP

trp 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 trp 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 trp GMP manufacturer or trp GMP API supplier for your needs.

trp CoA

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

trp CoA mostly includes findings from lab analyses of a specific batch. For each trp 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.

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