Compound: DL-Lysine
SMILES: O=C(O)C(N)CCCCN
InChIKey: KDXKERNSBIXSRK-UHFFFAOYSA-N
Synonyms: DL-Lysine, Lysine, DL-, (RS)-Lysine, (+-)-Lysine, UNII-AI4RT59273, CCRIS 8600, (+-)-2,6-Diaminohexanoic acid, AI4RT59273, DL-alpha,epsilon-Diaminocaproic acid, EINECS 200-740-6, DTXSID90859004, EC 200-740-6, RefChem:42679, DTXCID00196790, 200-740-6, 70-54-2, 2,6-diaminohexanoic acid, H-DL-Lys-OH, MFCD00064432, (R)-2,6-Diaminocaproic acid, (+/-)-2,6-Diaminocaproic acid, lysin, Lysine #, L-Lysine base, DL-Lysine base, 4,4,5,5-tetradeuterolysine, endolysin, alpha,epsilon-Diaminocaproic acid, NCGC00164527-01, Lys106, 2,6-diamino-hexanoic acid, SCHEMBL1645, lysine-4,4,5,5-d4, CHEMBL28328, (+/-)-LYSINE, orb1706209, orb3025618, SCHEMBL1066734, SCHEMBL1118713, SCHEMBL1939130, SCHEMBL7321504, SCHEMBL10002605, SCHEMBL11795443, SCHEMBL18059641, SCHEMBL18496157, SCHEMBL18691832, CHEBI:132486, 18746-72-0, HXB25266, HY-B2236, (4,4,5,5-(2)H4)lysine, BBL002414, EBC-44053, NSC620353, STK387123, AKOS005441647, CS-7806, NSC-620353, SB23228, DL-Lysine, purum, >=95.0% (NT), NCGC00164527-02, NCGC00166296-01, AS-56068, SY006101, (+/-)-2,6-DIAMINOHEXANOIC ACID, DB-055428, DB-057298, NS00003109, ST50824025, EN300-34227, DL-.ALPHA.,.EPSILON.-DIAMINOCAPROIC ACID, F208978, L001250, Q178430, SR-01000944856, SR-01000944856-1, ( inverted exclamation markA)-2,6-Diaminocaproic acid, 4D4E4503-F6A2-417D-A303-BDCAF08D1EBE, Z57127389, F8880-9052
Theoretical properties:
molecular_formula: C6H14N2O2
molecular_weight: 146.19 g/mol
exact_mass: 146.105527694 g/mol
formal_charge: 0
hydrogen_bond_donor_count: 3
hydrogen_bond_acceptor_count: 4
rotatable_bond_count: 5
heavy_atom_count: 10
topological_polar_surface_area: 89.3 Å²
isotope_atom_count: 0
covalently_bonded_unit_count: 1
Physical properties:
Descriptions:
{"pubchem": "Lysine is a diamino acid that is caproic (hexanoic) acid bearing two amino substituents at positions 2 and 6. It has a role as a Daphnia magna metabolite. It is a polar amino acid, an alpha-amino acid and a diamino acid. It contains a 4-aminobutyl group. It is functionally related to a hexanoic acid. It is a conjugate base of a lysinium(1+). It is a conjugate acid of a lysinate.", "chebi": "A diamino acid that is caproic (hexanoic) acid bearing two amino substituents at positions 2 and 6.", "chembl": "Unnamed Compound is a small molecule listed in the ChEMBL database but has not progressed to an approved clinical phase.", "wikipedia": "Lysine (symbol Lys or K) is an \u03b1-amino acid that is a precursor to many proteins. Lysine contains an \u03b1-amino group (which is in the protonated \u2212NH+3 form when the lysine is dissolved in water at physiological pH), an \u03b1-carboxylic acid group (which is in the deprotonated \u2212COO\u2212 form when the lysine is dissolved in water at physiological pH), and a side chain (CH2)4NH2 (which is partially protonated when the lysine is dissolved in water at physiological pH), and so it is classified as a basic, charged (in water at physiological pH), aliphatic amino acid. It is encoded by the codons AAA and AAG. Like almost all other amino acids, the \u03b1-carbon is chiral and lysine may refer to either enantiomer or a racemic mixture of both. For the purpose of this article, lysine will refer to the biologically active enantiomer L-lysine, where the \u03b1-carbon is in the S configuration. \nThe human body cannot synthesize lysine. It is essential in humans and must therefore be obtained from the diet. In organisms that synthesize lysine, two main biosynthetic pathways exist, the diaminopimelate and \u03b1-aminoadipate pathways, which employ distinct enzymes and substrates and are found in diverse organisms. Lysine catabolism occurs through one of several pathways, the most common of which is the saccharopine pathway.\nLysine plays several roles in humans, most importantly proteinogenesis, but also in the crosslinking of collagen polypeptides, uptake of essential mineral nutrients, and in the production of carnitine, which is key in fatty acid metabolism. Lysine is also often involved in histone modifications, and thus, impacts the epigenome. The \u03b5-amino group often participates in hydrogen bonding and as a general base in catalysis. The \u03b5-ammonium group (\u2212NH+3) is attached to the fourth carbon from the \u03b1-carbon, which is attached to the carboxyl (\u2212COOH) group.\nDue to its importance in several biological processes, a lack of lysine can lead to several disease states including defective connective tissues, impaired fatty acid metabolism, anaemia, and systemic protein-energy deficiency. In contrast, an overabundance of lysine, caused by ineffective catabolism, can cause severe neurological disorders.\nLysine was first isolated by the German biological chemist Ferdinand Heinrich Edmund Drechsel in 1889 from hydrolysis of the protein casein, and thus named it Lysin, from Greek  \u03bb\u03cd\u03c3\u03b9\u03c2 (lysis) 'loosening'. In 1902, the German chemists Emil Fischer and Fritz Weigert determined lysine's chemical structure by synthesizing it.\nThe one-letter symbol K was assigned to lysine for being alphabetically nearest, with L being assigned to the structurally simpler leucine, and M to methionine.\n\n"}