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Quality Level
Assay
≥98.0% (TLC)
optical activity
[α]/D 20.5±1.5°, c = 0.1 in 1 M HCl
storage temp.
2-8°C
SMILES string
Cl.CNCCCC[C@H](N)C(O)=O
InChI
1S/C7H16N2O2.ClH/c1-9-5-3-2-4-6(8)7(10)11;/h6,9H,2-5,8H2,1H3,(H,10,11);1H/t6-;/m0./s1
InChI key
AQELUQTVJOFFBN-RGMNGODLSA-N
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Biochem/physiol Actions
N ε-methyl-L-lysine was identified as a lysine analog with inhibitory effects on the growth and sporulation of Penicillium chrysogenum and benzyl-penicillin formation by mycelia.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Natural product communications, 6(5), 657-660 (2011-05-28)
The influence of monomethylated basic amino acids [NG-monomethyl-L-arginine (MMA) and Nepsilon-monomethyl-L-lysine (MML)] and ozone capturers (indigo carmine, d-limonene) on the antibacterial effect of the mycotoxins aflatoxins B1, B2, G1 and G2 was studied in BioArena, which is a complex bioautographic
The journal of physical chemistry. A, 111(32), 7753-7760 (2007-07-20)
The gas-phase structures of protonated and alkali-metal-cationized lysine (Lys) and epsilon-N-methyllysine (Lys(Me)) are investigated using infrared multiple photon dissociation (IRMPD) spectroscopy utilizing light generated by a free electron laser, in conjunction with ab initio calculations. IRMPD spectra of Lys.Li(+) and
European journal of biochemistry, 203(1-2), 81-87 (1992-01-15)
The complete amino acid sequence of glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus has been determined. The sequence was reconstructed by automated sequence analysis of peptides obtained after cleavage by trypsin, cyanogen bromide, Staphylococcus aureus V8 protease and pepsin.
Methylated lysines and 3-methylhistidine in myosin: tissue and developmental differences.
Methods in enzymology, 106, 287-295 (1984-01-01)
Journal of the American Chemical Society, 131(40), 14194-14195 (2009-09-24)
Lysine methylation is an important post-translational modification of histone proteins that defines epigenetic status and controls heterochromatin formation, X-chromosome inactivation, genome imprinting, DNA repair, and transcriptional regulation. Despite considerable efforts by chemical biologists to synthesize modified histones for use in
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