70-54-2

Basic information

• Product Name: DL-Lysine
• Synonyms: (+/-)-2,6-DIAMINOCAPROIC ACID;DL-2,6-DIAMINOHEXANOIC ACID;DL-LYSINE;DL-LYSINE BASE;H-DL-LYS-OH;(R,S)-2,6-Diamino-hexanoicacid;(RS)-Lysine;DL-α,ε-Diaminocaproicacid
• CAS NO: 70-54-2
• Molecular Formula: C₆H₁₄N₂O₂
• Molecular Weight: 146.19
• EINECS: 200-740-6
• Product Categories: Lysine [Lys, K];Amino Acids
• Mol File: 70-54-2.mol

Chemical Properties

• Melting Point: 170 °C (dec.)(lit.)
• Boiling Point: 265.81°C (rough estimate)
• Flash Point: 142.216 °C
• Appearance: /
• Density: 1,12 g/cm3
• Vapor Pressure: 0.000123mmHg at 25°C
• Refractive Index: 1.4650 (estimate)
• Storage Temp.: under inert gas (nitrogen or Argon) at 2–8 °C
• Solubility: Methanol (Slightly), Water (Slightly)
• PKA: 2.49±0.24(Predicted)
• CAS DataBase Reference: DL-Lysine(CAS DataBase Reference)
• NIST Chemistry Reference: DL-Lysine(70-54-2)
• EPA Substance Registry System: DL-Lysine(70-54-2)

Safety Data

• Safety Statements: 24/25
• WGK Germany: 3
• F: 3-10
• Hazardous Substances Data: 70-54-2(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
DL-Lysine is used as a precursor in the biosynthesis of Marcfortine A, a bioactive compound with potential therapeutic applications.
Used in Chemical Synthesis:
DL-Lysine is utilized as a building block in the synthesis of proteins, alkaloids, and other chemical compounds, playing a crucial role in various chemical and pharmaceutical processes.

InChI:InChI=1/C6H14N2O2/c7-4-2-1-3-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)

Upstream product

• 2100-17-6 4-pentenal 
• 627-76-9 alpha-aminopimelic acid 
• 10508-34-6 pentane-1,1,5-tricarboxylic acid 
• 71264-11-4 diethyl 2-acetamido-2-(3-cyanopropyl)malonate 
• 412033-98-8 acetylamino-(4-acetylamino-butyl)-malonic acid diethyl ester 
• 1700-05-6 6-benzamido-2-bromohexanoic acid 
• 5107-18-6 N⁶-benzoyl-lysine 
• 412036-78-3 6-benzoylamino-2-hydroxyimino-hexanoic acid ethyl ester 
• 1655-07-8 ethyl 2-oxocyclohexane carboxylate 
• 56-87-1 L-lysine 
• 13137-43-4 (+/-)-2,6-dibromohexanoic acid 
• 86088-67-7 ethyl 2-carbethoxy-2,6-diphthalimidohexanoate 
• 81505-57-9 C₃₆H₃₈N₂O₇ 
• 5457-30-7 4-phthalimido-1-iodobutane 

Downstream Products

• 56-87-1 L-lysine 
• 156-86-5 homoarginine 
• 2756-89-0 Δ¹-piperidine-2-carboxylic acid 
• 923-27-3 D-lysine 
• 32302-83-3 N-ε-benzyloxycarbonyl lysine 
• 32513-92-1 Nα,ε-dibenzoyl-D,L-lysine 
• 55592-85-3 DL-N,N-di-CBZ-lysine 
• 80913-74-2 N^α,N^ε-bis-[(2,4-dichloro-phenoxy)-acetyl]-DL-lysine 
• 64527-24-8 N²,N⁶-bis-(N-acetyl-sulfanilyl)-lysine 
• 32244-95-4 N⁶-(N-acetyl-sulfanilyl)-lysine 
• 140395-23-9 lysylchlorin-p₆ 
• 83793-79-7 6-Amino-2-(8-iodo-4-oxo-2-p-tolyloxymethyl-4H-quinazolin-3-yl)-hexanoic acid 
• 4433-40-3 5-hydroxymethyl uracil 
• 1124-84-1 cis-5,6-dihydroxy-5,6-dihydrothymine 

Relevant articles and documents

A method for preparing DL-lysine

The invention provides a method for preparing DL-lysine with chiral lysine salt as a raw material. The method specifically comprises the following steps: dissolving chiral lysine salt in an acetic acid water solution, adding salicylaldehyde or benzaldehyde as a catalyst, carrying out heating and racemization, removing solvents through vacuum distillation after racemization is completed, washing a residual solid with ethanol, obtaining DL-lysine salt, removing salt with an ion exchange column and carrying out concentration and decoloration, thus obtaining a DL-lysine solid. The preparation method has the advantages that the preparation method is lower in production cost and simple in process; pollution is not easily caused in the production process; the racemization rate of L-lysine hydrochloride can be 100%; the purity of the obtained DL-lysine finished product is more than 98%.

COMPOSITIONS AND METHODS FOR THE PREPARATION OF KIDNEY PROTECTIVE AGENTS COMPRISING AMIFOSTINE AND AMINO ACIDS

This invention relates to composition and method of preparation of AminoMedix? comprising of Amifostine, at least one amino acid (Arginine, Lysine, Histidine) with or without other pharmaceutically active compounds. The AminoMedix? composition can be applied for kidney protection during therapy using radiolabeled and non-radiolabeled compounds, contrast agents, chemotherapeutics, antibiotics and drugs showing nephrotoxic effect.

Lysine racemase from a lactic acid bacterium, Oenococcus oeni: Structural basis of substrate specificity

Oenococcus oeni, a lactic acid bacterium, possesses a lysine racemase, which has a specific activity towards basic amino acids. A comparison of amino acid residues around the active site suggested that Ile222 and Tyr354 of the Geobacillus stearothermophilus alanine racemase, which shares 60% sequence similarity with lysine racemase, were replaced by Thr224 and Trp355 in the O. oeni lysine racemase. T224I/W355Y double mutations significantly decreased the activity of lysine racemase, whereas I222T/Y354W double mutations endowed alanine racemase with lysine racemization activity. These results suggest that the two residues play an important role in lysine racemization.

Powder storage container

PROBLEM TO BE SOLVED: To prevent a sealing member from breaking away from a device body even when the sealing member is bent. SOLUTION: A toner replenishing type developing device 4Y, 4M, 4C or 4B comprises a developing device body 4a, and a sealing member 4e. The sealing member 4e comprises an insertion and removal part 41a which a toner replenishing pipe 13Y, 13M, 13C, or 13B is inserted into and removed from, and a bending part 41b which bends by the insertion of the replenishing pipe 13Y, 13M, 13C or 13B into the insertion and removal part 41a, and is restored to its original state by the removal of the toner replenishing pipe 13Y, 13M, 13C or 13B from the insertion and removal part 41a. The bending part 41b of the sealing member 4e is formed in such a manner that the thickness t2 thereof in the insertion direction of the toner replenishing pipe 13Y, 13M, 13C or 13B at the bending part 41b is smaller than the thickness t1 of the insertion and removal part 41a in the insertion direction of the toner replenishing pipe 13Y, 13M, 13C or 13B at the insertion and removal part 41a. COPYRIGHT: (C)2007,JPOandINPIT

Kinetics and mechanism of thermal decomposition of kynurenines and biomolecular conjugates: Ramifications for the modification of mammalian eye lens proteins

Thermal degradation reactions of kynurenine (KN), 3-hydroxykynurenine (3OHKN), and several adducts of KN, to amino acids and reduced glutathione (GSH) have been studied at physiological temperature. These compounds are all implicated in age-related mammalian eye lens cataract formation at the molecular level. The main reaction pathway for both KN and 3OHKN is deamination viaβ-elimination to carboxyketoalkenes CKA and 3OHCKA. These reactions show a weak pH dependence below pH values of ～8, and a strong pH dependence above this value. The 3OHKN structure deaminates at a faster rate than KN. A mechanism for the deamination reaction is proposed, involving an aryl carbonyl enol/enolate ion, that is strongly supported by the structural, kinetic, and pH data. The degradation of Lys, His, Cys and GSH adducts of the CKA moieties was also studied. The Lys adduct was found to be relatively stable over 200 h at 37 °C, while significant degradation was observed for the other adducts. The results are discussed in terms of known post-translational modification reactions of the lens proteins and compared to incubation studies involving KN and related compounds in the presence of proteins.

Compositions, kits, and methods relating to the human FEZ1 gene, a novel tumor suppressor gene

The invention relates to isolated polynucleotides homologous with a portion of one strand of the human tumor suppressor gene, FEZ1, and to the tumor suppressor protein encoded thereby, Fez1. The polynucleotides are useful, for example, as probes, primers, portions of expression vectors, and the like. The invention also includes diagnostic, therapeutic, cell proliferation enhancement, and screening methods which involve these polynucleotides and protein. The invention further includes kits useful for performing the methods of the invention.

Method for the selective and quantitative functionalization of immunoglobulin fab fragments, conjugate compounds obtained with the same and compositions thereof

The invention provides chemical conjugates between an immunoglobulin Fab fragment and molecular entities imparting diagnostic or therapeutic utility, whereby the only sites of conjugation on the Fab fragment are one or both of the sulfhydryl groups deriving from the selective and quantitative reduction of the inter-chain disulfide bond of said Fab fragment and whereby said molecular entities imparting diagnostic or therapeutic utility have at least one free sulfhydryl-reactive group, characterized in that the conjugation stoichiometric molar ratio molecular entity to Fab fragment is in the range from 0.95 to 1.05 or in the range from 1.95 to 2.05. The invention also provides a process for preparing said conjugates and pharmaceutical compositions thereof.

T-CELL SELECTIVE INTERLEUKIN-4 AGONISTS

The invention is directed to human IL-4 muteins numbered in accordance with wild-type IL-4 having T-cell activating activity, but having reduced endothelial cell activating activity. In particular, the invention is related to human IL-4 muteins wherein the surface-exposed residues of the D helix of the wild-type IL-4 are mutated whereby the resulting mutein causes T-cell proliferation, and causes reduced IL-6 secretion from HUVECs, relative to wild-type IL-4. This invention realizes a less toxic IL-4 mutant that allows greater therapeutic use of this interleukin. Further, the invention is directed to IL-4 muteins having single, double and triple mutations represented by the designators R121A, R121D, R121E, R121F, R121H, R121I, R121K, R121N, R121P, R121T, R121W; Y124A, Y124Q, Y124R, Y124S, Y124T; Y124A/S125A, T13D/R121E; and R121T/E122F/Y124Q, when numbered in accordance with wild-type IL-4 (His=1). The invention also includes polynucleotides coding for the muteins of the invention, vectors containing the polynucleotides, transformed host cells, pharmaceutical compositions comprising the muteins, and therapeutic methods of treatment.

(1 -> 3, 1 -> 4)-beta-glucanase of enhanced stability

A modified cereal (1→3,1→4)-β-glucanase is produced by the method of single point substitution in a native cereal (1→3,1→4)-β-glucanase enzyme, whereby the substitution: a) maintains enzyme specificity by conserving the active site groove of the native cereal (1→3,1→4)-β-glucanase enzyme; and b) effects increased thermostability over the native cereal (1→3,1→4)-β-glucanase enzyme by: i) replacing glycine by proline or alanine in helices of the cereal (1→3,1→4)-β-glucanase enzyme, in order to stiffen the enzyme amino acid chain and reduce entropy of the unfolded enzyme; ii) attaching negatively charged residues to N-termini of helices in the native cereal (1→3,1→4)-β-glucanase enzyme; iii) introducing ion pairs into the native cereal (1→3,1→4)-β-glucanase enzyme, to increase binding energy in the folded enzyme; iv) replacing lysine by arginine in the cereal (1→3,1→4)-β-glucanase enzyme, and thereby preventing lysine glycation and increasing hydrogen bonding with other parts of the enzyme; v) replacing, by glycine, an amino acid in the native cereal (1→3,1→4)-β-glucanase enzyme in which the main chain torsion angle about the N and Cα atoms is greater than 0°; or vi) creating cysteine pairs in the native cereal (1→3,1→4)-β-glucanase enzyme which can form disulphide bonds across the C and N terminals.

3-deoxyglucosone and skin

The invention relates to a method of removing 3-deoxyglucosone and other alpha-dicarbonyl sugars from skin. The invention further relates to methods of inhibiting production and function of 3-deoxyglucosone and other alpha-dicarbonyl sugars in skin. The invention also relates to methods of treating 3-deoxyglucosone and other alpha-dicarbonyl sugars associated diseases and disorders of skin.