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L-Lysine(CAS No. 56-87-1)

L-Lysine C6H14N2O2 (cas 56-87-1) Molecular Structure

56-87-1 Structure

Identification and Related Records

【CAS Registry number】
Hexanoic acid, 2,6-diamino-, (S)-
Lysine, L- (8CI)
Aminutrin, 6-amino-
L-Lysine (USAN)
(S)-alpha,epsilon-diaminocaproic acid
L-Lysine (9CI)
(S)-2,6-diaminohexanoic acid
2,6-Diaminohexanoic acid, (S)-
L-Norleucine, 6-amino-
Lysine acid
Lysine, L-
LYS (IUPAC abbreviation)
L-Lysine Base
L-Lysine Free Base
L-Lysine alkali
L-Lysine Feed Grade
L-Lysine,L-Glutamic acid,L-Arginine,L-Cystine
L -lysine
L-Lysine 50% Solution
【Molecular Formula】
C6H14N2O2 (Products with the same molecular formula)
【Molecular Weight】
【Canonical SMILES】
【Isomers smiles】
【MOL File】

Chemical and Physical Properties

white or almost white crystalline powder
【Melting Point】
215℃ (dec.)
【Boiling Point】
【Refractive Index】
26 ° (C=2, 5mol/L HCl)
【Flash Point】
H2O: 0.1 g/mL, clear, colorless
H2O: 0.1 g/mL, clear, colorless
Needles from water, hexagonal plates from dilute alcohol
Colorless crystals
Stable. Incompatible with strong oxidizing agents.
【Storage temp】
Store at RT.
【Spectral properties】
Specific optical rotation: +14.6 at 20 deg C/D (c = 6.5); +25.9 at 23 deg C/D (c = 2 in 6.0N HCl)
IR: 18007 (Sadtler Research Laboratories IR Grating Collection)
1H NMR: 8213 (Sadtler Research Laboratories Spectral Collection)
13C NMR: 479 (Stothers, Cabon-13 NMR Spectroscopy, Academic Press, New York)
MASS: 26152 (NIST/EPA/MSDC Mass Spectral Database, 1990 version)
【Computed Properties】
Molecular Weight:146.18756 [g/mol]
Molecular Formula:C6H14N2O2
H-Bond Donor:3
H-Bond Acceptor:4
Rotatable Bond Count:5
Exact Mass:146.105528
MonoIsotopic Mass:146.105528
Topological Polar Surface Area:89.3
Heavy Atom Count:10
Formal Charge:0
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
Feature 3D Acceptor Count:2
Feature 3D Donor Count:2
Feature 3D Anion Count:1
Feature 3D Cation Count:2
Effective Rotor Count:5
Conformer Sampling RMSD:0.6
CID Conformer Count:93

Safety and Handling

【Hazard Codes】
Xi: Irritant;
【Safety Statements 】
An experimental teratogen. Experimental reproductive effects. When heated to decomposition it emits toxic fumes of NOx.
As DL- and L-lysine monohydrochloride.
USP and FCC grades /lysine hydrochloride/
【Exposure Standards and Regulations】
L-Lysine is a food additive permitted for direct addition to food for human consumption, as long as 1) the quantity of the substance added to food does not exceed the amount reasonably required to accomplish its intended physical, nutritive, or other technical effect in food, and 2) any substance intended for use in or on food is of appropriate food grade and is prepared and handled as a food ingredient.
Drug products containing certain active ingredients offered over-the-counter (OTC) for certain uses. A number of active ingredients have been present in OTC drug products for various uses, as described below. However, based on evidence currently available, there are inadequate data to establish general recognition of the safety and effectiveness of these ingredients for the specified uses: lysine hydrochloride is included in digestive aid drug products. /Lysine hydrochloride/
Drug products containing certain active ingredients offered over-the-counter (OTC) for certain uses. A number of active ingredients have been present in OTC drug products for various uses, as described below. However, based on evidence currently available, there are inadequate data to establish general recognition of the safety and effectiveness of these ingredients for the specified uses: lysine is included in weight control drug products.
Drug products containing certain active ingredients offered over-the-counter (OTC) for certain uses. A number of active ingredients have been present in OTC drug products for various uses, as described below. However, based on evidence currently available, there are inadequate data to establish general recognition of the safety and effectiveness of these ingredients for the specified uses: lysine hydrochloride is included in weight control drug products. /Lysine hydrochloride/
Lysine used as a nutrient and/or dietary supplement in animal drugs, feeds, and related products is generally recognized as safe when used in accordance with good manufacturing or feeding practice.

?The L-Lysine, with the cas registry number 56-87-1, has the IUPAC name of (2S)-2,6-diaminohexanoic acid. This is a kind of white or almost white crystalline powder with no odour, and it is stable chemically but incompatible with strong oxidizing agents. Besides, its product categories are various, including? Amino Acid Derivatives; Lysine [Lys, K]; Amino Acids; alpha-Amino Acids; Biochemistry; Nutritional Supplements; Amino Acids.

The characteristics of this kind of chemical are as follows: (1)ACD/LogP: -1.04; (2)# of Rule of 5 Violations: 1; (3)ACD/LogD (pH 5.5): -4.54; (4)ACD/LogD (pH 7.4): -4.5; (5)ACD/BCF (pH 5.5): 1; (6)ACD/BCF (pH 7.4): 1; (7)ACD/KOC (pH 5.5): 1; (8)ACD/KOC (pH 7.4): 1; (9)#H bond acceptors: 4; (10)#H bond donors: 5; (11)#Freely Rotating Bonds: 7; (12)Polar Surface Area: 32.78; (13)Index of Refraction: 1.503; (14)Molar Refractivity: 38.43 cm3; (15)Molar Volume: 129.9 cm3; (16)Polarizability: 15.23×10-24 cm3; (17)Surface Tension: 51.5 dyne/cm; (18)Density: 1.125 g/cm3; (19)Flash Point: 142.2 °C; (20)Enthalpy of Vaporization: 60.75 kJ/mol; (21)Boiling Point: 311.5 °C at 760 mmHg; (22)Vapour Pressure: 0.000123 mmHg at 25°C; (23)Exact Mass: 146.105528; (24)MonoIsotopic Mass: 146.105528; (25)Topological Polar Surface Area: 89.3; (26)Heavy Atom Count: 10; (27)Formal Charge: 0; (28)Complexity: 106.

The production methods of this chemical are as follows: (1) Free L-Lysine could be obtained from L-lysine hydrochloride. (2) Firstly prepare raw material of Red blood cells, and then suspend it? in sulfuric acid solution; Secondly, use the calcium hydroxide to precipitate, and then go through the washing, crystallization to get L-Lysine (CAS NO.56-87-1). (3) Synthesis method: caprolactam and furfural as the raw material.

As to its usage, it is widely applied in many ways. It could be used as the nutrition enhancer which could enhance the lysine in intensified [enriched] food; It could also used in biochemistry? to cure the symptom of malnutrition, inappetence and hypoplasia; And it could be as the Aminoacetic Acid, and the feed additives.

Below are the safety information of this chemical: Being a kind of irritant chemical, it may cause inflammation to the skin or other mucous membranes, so you should avoid contacting with skin and eyes while using.

Additionally, the following datas could be converted into the molecular structure:
(1)Canonical SMILES: C(CCN)CC(C(=O)O)N
(2)Isomeric SMILES: C(CCN)C[C@@H](C(=O)O)N
(3)InChI: InChI=1S/C6H14N2O2/c7-4-2-1-3-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)/t5-/m0/s1

【Octanol/Water Partition Coefficient】
log Kow = -3.05
【Disposal Methods】
SRP: Criteria for land treatment or burial (sanitary landfill) disposal practices are subject to significant revision. Prior to implementing land disposal of waste residue (including waste sludge), consult with environmental regulatory agencies for guidance on acceptable disposal practices.

Use and Manufacturing

【Use and Manufacturing】
Methods of Manufacturing

Isolation from acid-hydrolyzed proteins (casein, fibrin or blood corpuscle paste)
Extraction of natural proteins, synthetically by fermentation of glucose or other carbohydrates and by synthesis from caprolactum
The usual raw material for the fermentation production of L-lysine is molasses...high performance microbes belong to the species Corynebacterium glutamicum or Brevibactrium lactofermentum
A process combining chemical and microbiological techniques for the production of L-lysine was introduced by Toray Industries; /in this process/, alpha-amino-e-caprolactam (ACL) is formed from cyclohexanol... this intermediate is then hydrolyzed with L-ACL-hydrolase to yield L-lysine
U.S. Production

World market for L-lysine in 1982: 34,000 tons, in 1984: 32,000 tons /free acid and hydrochloride/
World market for L-lysine in 1987: 100,000 tons /free acid and hydrochloride/
Production volumes for non-confidential chemicals reported under the Inventory Update Rule. Year Production Range (pounds) 1986 No Reports 1990 No Reports 1994 10 thousand - 500 thousand 1998 10 thousand - 500 thousand 2002 No Reports
Consumption Patterns

L-Lysine /hydrochloride/ is used almost exclusively to improve the nutritive value of animal feeds

Food enrichment, nutrient.

Biomedical Effects and Toxicity

【Therapeutic Uses】
Lysine appears to have antiviral, anti-osteoporotic, cardiovascular, and lipid-lowering effects, although more controlled human studies are needed.
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.
/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. [Baier S, et al; J Parenter Enteral Nutr 33 (1): 71-82 (2009). Available from, as of March 23, 2010:]
【Biomedical Effects and Toxicity】
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/
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/
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/
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/
Five 28-day-old piglets implanted with arterial, venous, and portal catheters and with an ultrasonic portal flow probe were given an oral bolus feeding of a milk formula containing a trace quantity of intrinsically 15N-labeled soy protein and a continuous intravenous infusion of U-(13)C-lysine for 8 hr. Total lysine use by the PDV was maximal 1 hr after the meal (891 umol/ kg/hr) and was predominantly of dietary origin (89%), paralleling the enteral delivery of dietary lysine. Intestinal lysine use returned to a low level after 4 hr postprandially and was derived exclusively from the arterial supply until 8 hr. Cumulative systemic appearance of dietary lysine reached 44 and 80% of the ingested amount 4 and 8 hr after the meal, respectively, whereas the PDV first-pass use of dietary lysine was 55 and 32% of the intake for these two periods, respectively ... The first-pass utilization rate of dietary lysine by the PDV is directly increased by the enteral lysine availability and ... is higher with a bolus than with continuous oral feeding. [Bos C, et al; Am J Physiol Endocrinol Metab 285 (6): 1246-57 (2003). Available from, as of March 23, 2010:] PubMed Abstract
It was noted that blood concentrations could be considerably higher when amino acids were consumed as supplements as opposed to a component of protein in food.
Although it seems clear that the efficiency of dietary protein digestion (in the sense of removal of amino acids from the small intestinal lumen) is high, there is now good evidence to show that nutritionally significant quantities of indispensable amino acids are metabolized by the tissues of the splanchnic bed, including the mucosal cells of the intestine. Thus, less than 100% of the amino acids removed from the intestinal lumen appear in the peripheral circulation, and the quantities that are metabolized by the splanchnic bed vary among the amino acids, with intestinal threonine metabolism being particularly high. /Amino acids/

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