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1. Acetate, Lysine
2. Enisyl
3. L Lysine
4. L-lysine
5. Lysine Acetate
6. Lysine Hydrochloride
1. L-lysine
2. 56-87-1
3. Lysine Acid
4. H-lys-oh
5. (2s)-2,6-diaminohexanoic Acid
6. (s)-lysine
7. Aminutrin
8. L-(+)-lysine
9. (s)-2,6-diaminohexanoic Acid
10. Alpha-lysine
11. Poly-l-lysine
12. Hydrolysin
13. Lysinum [latin]
14. L-lys
15. Lisina [spanish]
16. L-norleucine, 6-amino-
17. Lysine, L-
18. Lysinum
19. (s)-alpha,epsilon-diaminocaproic Acid
20. Lysine [usan:inn]
21. (s)-2,6-diaminocaproic Acid
22. Lys (iupac Abbreviation)
23. L-2,6-diaminocaproic Acid
24. 25104-18-1
25. Hexanoic Acid, 2,6-diamino-, (s)-
26. Lys
27. Chebi:18019
28. A-lysine
29. 2,6-diaminohexanoic Acid, (s)-
30. L-lysin
31. Brn 1722531
32. Ai3-26523
33. (+)-s-lysine
34. 6-ammonio-l-norleucine
35. 12798-06-0
36. Lysin
37. L-lysine Base
38. K3z4f929h6
39. Hsdb 2108
40. L-2,6-diaminocaproate
41. Lisina
42. L-lysine, Monoacetate
43. Mfcd00064433
44. 3h-lysine
45. 2,6-diaminohexanoate
46. Einecs 200-294-2
47. Lysina
48. Unii-k3z4f929h6
49. L-lysine, Labeled With Tritium
50. Ketporofen Lysine
51. .alpha.-lysine
52. 1ozv
53. 1yxd
54. 3h-l-lysine
55. 6-amino-aminutrin
56. Ncgc00164527-01
57. Poly-(l-lysine)
58. H-lys
59. (-)-lysine
60. 6-amino-l-norleucine
61. A,e-diaminocaproic Acid
62. Lysine (usan/inn)
63. Alpha-poly-(l-lysine)
64. L-2,6-diainohexanoate
65. Lysine [vandf]
66. Lysine [hsdb]
67. Lysine [inci]
68. Lysine [usan]
69. Lysine [inn]
70. L-lysine [fhfi]
71. Lysine [who-dd]
72. (s)-a,e-diaminocaproate
73. Lysine [ii]
74. Lysine [mi]
75. Lysine [mart.]
76. Dsstox_cid_3232
77. L-lysine, >=97%
78. Bmse000043
79. Bmse000914
80. Epitope Id:136017
81. (s)-2,6-diaminohexanoate
82. L-2,6-diainohexanoic Acid
83. Chembl8085
84. Dsstox_rid_76935
85. Dsstox_gsid_23232
86. Gtpl724
87. (s)-2,6-diamino-hexanoate
88. (s)-a,e-diaminocaproic Acid
89. 4-04-00-02717 (beilstein Handbook Reference)
90. L-lysine, Analytical Standard
91. L-lysine, >=98%, Fg
92. Dtxsid6023232
93. (s)-2,6-diamino-hexanoic Acid
94. L-lysine, >=98% (tlc)
95. Bdbm217367
96. (2s)-2,6-diamino-hexanoic Acid
97. Act02654
98. Hy-n0469
99. L-h2n(ch2)4ch(nh2)cooh
100. Zinc1532522
101. Tox21_112158
102. Ethyl3,5-dichloro-4-propoxybenzoate
103. S5630
104. .alpha.,.epsilon.-diaminocaproic Acid
105. Akos006239081
106. Akos015855172
107. Ccg-266180
108. Cs-w019758
109. Db00123
110. Cas-56-87-1
111. L-lysine Solution, Purum, 50% In H2o
112. Ncgc00166296-02
113. 20166-34-1
114. Ac-14492
115. As-11733
116. Tyrosine Impurity B [ep Impurity]
117. (s)-.alpha.,.epsilon.-diaminocaproic Acid
118. L-lysine, Crystallized, >=98.0% (nt)
119. Am20100376
120. L0129
121. L-lysine, Vetec(tm) Reagent Grade, >=98%
122. A20652
123. C00047
124. D02304
125. 064l433
126. A904498
127. A919375
128. J-521651
129. (s)-2,6-diaminocaproic Acid;(s)-(+)-lysine;lysine
130. Q20816880
131. F0001-1472
132. 0013cd6b-1671-4369-b1be-f531611e50c7
| Molecular Weight | 146.19 g/mol |
|---|---|
| Molecular Formula | C6H14N2O2 |
| XLogP3 | -3 |
| Hydrogen Bond Donor Count | 3 |
| Hydrogen Bond Acceptor Count | 4 |
| Rotatable Bond Count | 5 |
| Exact Mass | 146.105527694 g/mol |
| Monoisotopic Mass | 146.105527694 g/mol |
| Topological Polar Surface Area | 89.3 Ų |
| Heavy Atom Count | 10 |
| Formal Charge | 0 |
| Complexity | 106 |
| 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 |
Lysine appears to have antiviral, anti-osteoporotic, cardiovascular, and lipid-lowering effects, although more controlled human studies are needed.
PDR Network, LLC. PDR for Nonprescription Drugs, Dietary Supplements, and Herbs. 31st Ed. PDR Network, LLC, Montvale, NJ. 2010 p. 596
Unproven uses: The most common use of supplemental lysine is for preventing and treating episodes of herpes simplex virus. Lysine has been used in conjunction with calcium to prevent and treat osteoporosis. It has also been used for treating pain, aphthous ulcers, migraine attacks, rheumatoid arthritis, and opiate withdrawal. Many "body-building" formulations contain lysine to aid in muscle repair.
PDR Network, LLC. PDR for Nonprescription Drugs, Dietary Supplements, and Herbs. 31st Ed. PDR Network, LLC, Montvale, NJ. 2010 p. 596
/Experimental Therapy/ A major contributing factor to the loss of mobility in elderly people is the gradual and continuous loss of lean body mass ... Elderly (76 +/-1.6 years) women (n = 39) and men (n = 38) were recruited for a double-blinded controlled study. Study participants were randomly assigned to either an isonitrogenous control-supplement (n = 37) or a treatment-supplement (HMB/Arg/Lys) consisting of beta-hydroxy-beta-methylbutyrate, L-arginine, and L-lysine (n = 40) for the 1-year study ... In subjects taking the HMB/Arg/Lys supplement, lean tissue increased over the year of study while in the control group, lean tissue did not change ... Consumption of a simple amino acid-related cocktail increased protein turnover and lean tissue in elderly individuals in a year-long study.
PMID:19164608 Baier S, et al; J Parenter Enteral Nutr 33 (1): 71-82 (2009).
Supplementation of meals with low doses of oral lysine improved fasting plasma lysine concentrations in 27 Finnish patients with lysinuric protein intolerance (LPI) without causing hyperammonemia or other recognizable side effects during 12 months of follow-up. In conclusion, low-dose oral lysine supplementation is potentially beneficial to patients with LPI and can be started safely at an early age.
PMID:17224331 Tanner LM, et al; Metab Clin Exper 56 (2): 185-9 (2007).
Patients with hypercholesterolemia should be aware that supplemental lysine has been linked to increased cholesterol levels in animal studies. However, other studies have shown lysine can also decrease cholesterol levels.
PDR Network, LLC. PDR for Nonprescription Drugs, Dietary Supplements, and Herbs. 31st Ed. PDR Network, LLC, Montvale, NJ. 2010 p. 596
Adverse reactions: renal dysfunction, including Fanconi's syndrome and renal failure, has been reported.
PDR Network, LLC. PDR for Nonprescription Drugs, Dietary Supplements, and Herbs. 31st Ed. PDR Network, LLC, Montvale, NJ. 2010 p. 596
L-lysine ibuprofen /was given/ to a preterm infant with respiratory distress to induce closure of a patent ductus arteriosus, and the infant experienced pulmonary hypertension. Only 3 cases of pulmonary hypertension following early administration of an ibuprofen solution buffered with tromethamine have previously been reported. However, this severe side effect has never been observed in multicentre, randomized, double-blind controlled trials, nor in recent reviews or meta-analyses of L-lysine ibuprofen use.
PMID:16785458 Full text: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1475921 Bellini C, et al; Can Med Assoc J 174 (13): 1843-4 (2006).
Supplemental lysine has putative anti-herpes simplex virus activity. There is preliminary research suggesting that it may have some anti-osteoporotic activity.
Insures the adequate absorption of calcium; helps form collagen ( which makes up bone cartilage & connective tissues); aids in the production of antibodies, hormones & enzymes. Recent studies have shown that Lysine may be effective against herpes by improving the balance of nutrients that reduce viral growth. A deficiency may result in tiredness, inability to concentrate, irritability, bloodshot eyes, retarded growth, hair loss, anemia & reproductive problems.
B - Blood and blood forming organs
B05 - Blood substitutes and perfusion solutions
B05X - I.v. solution additives
B05XB - Amino acids
B05XB03 - Lysine
Absorption
Absorbed from the lumen of the small intestine into the enterocytes by an active transport process
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
About 11 to 15 g of nitrogen are excreted each day in the urine of a healthy adult consuming 70 to 100 g of protein, mostly in the form of urea, with smaller contributions from ammonia, uric acid, creatinine, and some free amino acids. These are the end products of protein metabolism, with urea and ammonia arising from the partial oxidation of amino acids. Uric acid and creatinine are indirectly derived from amino acids as well. The removal of nitrogen from the individual amino acids and its conversion to a form that can be excreted by the kidney can be considered as a two-part process. The first step usually takes place by one of two types of enzymatic reactions: transamination or deamination. Transamination is a reversible reaction that uses ketoacid intermediates of glucose metabolism (e.g., pyruvate, oxaloacetate, and alpha-ketoglutarate) as recipients of the amino nitrogen. Most amino acids can take part in these reactions, with the result that their amino nitrogen is transferred to just three amino acids: alanine from pyruvate, aspartate from oxaloacetate, and glutamate from alpha-ketoglutarate. Unlike many amino acids, branched-chain amino acid transamination occurs throughout the body, particularly in skeletal muscle. Here the main recipients of amino nitrogen are alanine and glutamine (from pyruvate and glutamate, respectively), which then pass into the circulation. These serve as important carriers of nitrogen from the periphery (skeletal muscle) to the intestine and liver. In the small intestine, glutamine is extracted and metabolized to ammonia, alanine, and citrulline, which are then conveyed to the liver via the portal circulation. Nitrogen is also removed from amino acids by deamination reactions, which result in the formation of ammonia. A number of amino acids can be deaminated, either directly (histidine), by dehydration (serine, threonine), by way of the purine nucleotide cycle (aspartate), or by oxidative deamination (glutamate). ... Glutamate is also formed in the specific degradation pathways of arginine and lysine. Thus, nitrogen from any amino acid can be funneled into the two precursors of urea synthesis, ammonia and aspartate. /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. 603-604, 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-Lysine (7 total), please visit the HSDB record page.
Hepatic
Like other amino acids, the metabolism of free lysine follows two principal paths: protein synthesis and oxidative catabolism. It is required for biosynthesis of such substances as carnitine, collage, and elastin.
PDR Network, LLC. PDR for Nonprescription Drugs, Dietary Supplements, and Herbs. 31st Ed. PDR Network, LLC, Montvale, NJ. 2010 p. 596
Oxidative deamination or transamination of l-lysine /yields/ alpha-keto-epsilon-aminocaproic acid; decarboxylation of l-lysine /yields/ cadaverine. /From table/
Fenaroli's Handbook of Flavor Ingredients. Volume 2. Edited, translated, and revised by T.E. Furia and N. Bellanca. 2nd ed. Cleveland: The Chemical Rubber Co., 1975., p. 830
Once the amino acid deamination products enter the tricarboxylic acid (TCA) cycle (also known as the citric acid cycle or Krebs cycle) or the glycolytic pathway, their carbon skeletons are also available for use in biosynthetic pathways, particularly for glucose and fat. Whether glucose or fat is formed from the carbon skeleton of an amino acid depends on its point of entry into these two pathways. If they enter as acetyl-CoA, then only fat or ketone bodies can be formed. The carbon skeletons of other amino acids can, however, enter the pathways in such a way that their carbons can be used for gluconeogenesis. This is the basis for the classical nutritional description of amino acids as either ketogenic or glucogenic (ie, able to give rise to either ketones [or fat] or glucose). Some amino acids produce both products upon degradation and so are considered both ketogenic and glucogenic. /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. 606, 2009. Available from, as of March 10, 2010: https://www.nap.edu/catalog/10490.html
... Rates of lysine metabolism in fetal sheep during chronic hypoglycemia and following euglycemic recovery /were compared with/ results with normal, age-matched euglycemic control fetuses to explain the adaptive response of protein metabolism to low glucose concentrations. Restriction of the maternal glucose supply to the fetus lowered the net rates of fetal (umbilical) glucose (42%) and lactate (36%) uptake, causing compensatory alterations in fetal lysine metabolism. The plasma lysine concentration was 1.9-fold greater in hypoglycemic compared with control fetuses, but the rate of fetal (umbilical) lysine uptake was not different. In the hypoglycemic fetuses, the lysine disposal rate also was higher than in control fetuses due to greater rates of lysine flux back into the placenta and into fetal tissue. The rate of CO2 excretion from lysine decarboxylation was 2.4-fold higher in hypoglycemic than control fetuses, indicating greater rates of lysine oxidative metabolism during chronic hypoglycemia. No differences were detected for rates of fetal protein accretion or synthesis between hypoglycemic and control groups, although there was a significant increase in the rate of protein breakdown (p < 0.05) in the hypoglycemic fetuses, indicating small changes in each rate. This was supported by elevated muscle specific ubiquitin ligases and greater concentrations of 4E-BP1. Euglycemic recovery after chronic hypoglycemia normalized all fluxes and actually lowered the rate of lysine decarboxylation compared with control fetuses (p < 0.05). These results indicate that chronic hypoglycemia increases net protein breakdown and lysine oxidative metabolism, both of which contribute to slower rates of fetal growth over time. Furthermore, euglycemic correction for 5 days returns lysine fluxes to normal and causes an overcorrection of lysine oxidation.
PMID:19190258 Full text: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2670627 Limesand SW, et al; Am J Physiol Endocrinol Metab 296 (4): 879-87 (2009).
Proteins of the herpes simplex virus are rich in L-arginine, and tissue culture studies indicate an enhancing effect on viral replication when the amino acid ratio of L-arginine to lysine is high in the tissue culture media. When the ratio of L-lysine to L-arginine is high, viral replication and the cytopathogenicity of herpes simplex virus have been found to be inhibited. L-lysine may facilitate the absorption of calcium from the small intestine.
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. /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. 602, 2009. Available from, as of March 10, 2010: https://www.nap.edu/catalog/10490.html
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