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
• Article Data: 106

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

DL-Lysine is a racemic mixture of the D and L enantiomers of lysine amino acid. Used in the synthesis of proteins, alkaloids and other chemical compounds. Used as a precursor in biosynthesis of Marcfortine A.

Definition

ChEBI: A diamino acid that is caproic (hexanoic) acid bearing two amino substituents at positions 2 and 6.

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

Upstream product

• 412033-98-8 acetylamino-(4-acetylamino-butyl)-malonic acid diethyl ester 
• 81505-57-9 C₃₆H₃₈N₂O₇ 
• 740-63-6 Nα-benzoyl-glycyl-L-lysine 
• 2100-17-6 4-pentenal 
• 20537-88-6 amifostine 
• 923-27-3 D-lysine 
• 657-27-2 L-Lysine hydrochloride 
• 60644-15-7 N-acetylpiperidine-2-carbonitrile 
• 100-70-9 2-Cyanopyridine 
• 6313-34-4 4-hydroxy-3-nitro-benzene sulfonic acid sodium salt 
• 412037-28-6 (4-benzoylamino-butyl)-malonic acid diethyl ester 
• 81505-48-8 (D,L)-N-Cbz-ε-hydroxynorleucine benzyl ester 
• 32245-65-1 (D,L)-Cbz-ε-hydroxynorleucine 
• 5462-80-6 rac-6-hydroxynorleucine 

Downstream Products

• 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 
• 13514-92-6 6-Hydroxydihydrothymine 
• 696-04-8 5,6-dihydrothymine 
• 17929-90-7 3-aminoazepan-2-one 
• 123-38-6 propionaldehyde 
• 687-64-9 DL-lysine methyl ester 
• 80913-74-2 N^α,N^ε-bis-[(2,4-dichloro-phenoxy)-acetyl]-DL-lysine 
• 32302-83-3 N-ε-benzyloxycarbonyl lysine 
• 56-87-1 L-lysine 

Relevant articles and documents

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.

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.