CHEBI:43997 - N⁶,N⁶-dimethyl-L-lysine

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ChEBI Name N6,N6-dimethyl-L-lysine ChEBI ID CHEBI:43997 ChEBI ASCII Name N(6),N(6)-dimethyl-L-lysine Definition An L-lysine derivative comprising L-lysine having two methyl substituents attached to the side-chain amino group. Stars This entity has been manually annotated by the ChEBI Team. Secondary ChEBI IDs CHEBI:43992, CHEBI:21855 Supplier Information ZINC000002579066 Download Molfile XML SDF Find compounds which contain this structure Find compounds which resemble this structure Take structure to the Advanced Search Formula C8H18N2O2 Net Charge 0 Average Mass 174.24070 Monoisotopic Mass 174.13683 InChI InChI=1S/C8H18N2O2/c1-10(2)6-4-3-5-7(9)8(11)12/h7H,3-6,9H2,1-2H3,(H,11,12)/t7-/m0/s1 InChIKey XXEWFEBMSGLYBY-ZETCQYMHSA-N SMILES CN(C)CCCC[C@H](N)C(O)=O Roles Classification Chemical Role(s): Bronsted base A molecular entity capable of accepting a hydron from a donor (Bronsted acid). (via organic amino compound ) Bronsted acid A molecular entity capable of donating a hydron to an acceptor (Bronsted base). (via oxoacid ) View more via ChEBI Ontology ChEBI Ontology Outgoing N6,N6-dimethyl-L-lysine (CHEBI:43997) is a L-lysine derivative (CHEBI:25095) N6,N6-dimethyl-L-lysine (CHEBI:43997) is a non-proteinogenic L-α-amino acid (CHEBI:83822) N6,N6-dimethyl-L-lysine (CHEBI:43997) is conjugate base of N6,N6-dimethyl-L-lysinium (CHEBI:193107) Incoming N6,N6-dimethyl-L-lysinium (CHEBI:193107) is conjugate acid of N6,N6-dimethyl-L-lysine (CHEBI:43997) N6,N6-dimethyl-L-lysine residue (CHEBI:61969) is substituent group from N6,N6-dimethyl-L-lysine (CHEBI:43997) IUPAC Name N6,N6-dimethyl-L-lysine Synonyms Sources (S)-2-amino-6-dimethylaminohexanoic acid ChEBI Epsilon N-dimethyllysine ChemIDplus Lys(Me2) ChEBI N(6),N(6)-Dimethyl-L-lysine ChemIDplus N6,N6-dimethyllysine ChEBI Nε,Nε-dimethyl-L-lysine ChEBI Nε,Nε-dimethyllysine ChEBI Nε-dimethyl-L-lysine ChEBI Nε-dimethyllysine ChEBI Manual Xref Database MLY PDBeChem View more database links Registry Numbers Types Sources 2259-86-1 CAS Registry Number ChemIDplus 2355193 Reaxys Registry Number Reaxys Citations Lobet Y, Lhoest J, Colson C (1989) Partial purification and characterization of the specific protein-lysine N-methyltransferase of YL32, a yeast ribosomal protein. Biochimica et biophysica acta 997, 224-231 [PubMed:2504290] [show Abstract] YL23 and YL32 are two of the three most heavily methylated ribosomal proteins of Saccharomyces cerevisiae. Using an in vitro assay, it was determined that they are methylated by two distinct enzymes. The protein-lysine N-methyltransferase that methylates YL32 was partially purified by affinity and ion-exchange chromatography. Its molecular mass was estimated to be 82 kDa, and its isoelectric point to be 4.45. Optimum activity was expressed at pH 7.5, and the enzyme was irreversibly inactivated at pH lower than 5.0. The Km of the enzyme for AdoMet is 1.7 +/- 0.4 microM, and the Ki toward AdoHcy was 0.71 microM. Formation of epsilon-N-dimethyllysine was observed to occur in two steps via epsilon-N-monomethyllysine. Like other protein-lysine N-methyltransferases, the methylase of YL32 exhibits a high substrate specificity. Paolantonacci P, Lawrence F, Lederer F, Robert-Gero M (1986) Protein methylation and protein methylases in Leishmania donovani and Leishmania tropica promastigotes. Molecular and biochemical parasitology 21, 47-54 [PubMed:3773934] [show Abstract] We studied the content of acid-stable methylated amino acids of soluble proteins in promastigotes of Leishmania donovani and L. tropica. epsilon-N-Trimethyllysine and NG,NG-dimethylarginine were found in both Leishmania species after culture in the presence of [methyl-14C]methionine. In addition, 3-N-methylhistidine was found only in L. tropica and epsilon-N-dimethyllysine only in proteins of L. donovani. As sinefungin, an antileishmanial nucleoside antibiotic, is a known transmethylase inhibitor, its effect on protein methylation was studied, in whole cells and in vitro. In the first case the drug had no effect on the content of methylated amino acid residues of soluble proteins. In vitro, histone methylation by crude extracts was studied at pH 7.2 and 9.0, known in other organisms as optimum pH values for arginine and lysine methylation, respectively. Surprisingly, arginine methylation by extracts of L. donovani was the same at both pH values while lysine residues were more efficiently methylated at pH 7.2 than at pH 9 by the extracts of the two species. These results indicate that the properties of protein methylases I and III of these parasites are different from those of other organisms hitherto studied. The inhibition constants of sinefungin for the leishmanial protein methylases were weak in comparison with those for enzymes from other sources, with the exception of the constant of L. donovani enzyme at pH 9. Sherry AD, Teherani J (1983) Physical studies of 13C-methylated concanavalin A. pH- and Co2+-induced nuclear magnetic resonance shifts. The Journal of biological chemistry 258, 8663-8669 [PubMed:6863304] [show Abstract] Concanavalin A has been reductively methylated using [13C]formaldehyde and NaCNBH3 and examined by 13C NMR. The chemical modification does not alter the metal ion or saccharide binding properties of the protein nor the associating of dimers to form tetramers above pH 6. Eleven of the 12 N epsilon,N-dimethyllysines appear as a broad unresolved group of resonances at pH 5.6, while one N epsilon,N-dimethyllysine (tentatively assigned to Lys 101) gives rise to two resolved methyl resonances as a result of forming a salt bridge with Asp 203 (Reeke, G. N., Jr., Becker, J. W., and Edelman, G. M. (1975) J. Biol. Chem. 250, 1525-1547). The NH2-terminal N alpha,N-dimethylalanine appears as a unique resonance and titrates with a pKa of 7.9. The chemical shift degeneracy of the N epsilon,N-dimethyllysine is lifted when Co2+ is bound in the S1 site of the protein. These resonances sharpen and shift downfield differentially with increasing pH until eight of 12 N epsilon,N-dimethyllysine resonances are resolved at pH 10. A comparison of the expected Co2+-induced shift at each lysine based upon their crystal coordinates and previous Co2+-histidine shift data (Carver, J. P., Barber, B. H., and Fuhr, B. J. (1977) J. Biol. Chem. 252, 3141-3146) with those observed in the N epsilon,N-dimethyllysine resonances has allowed a tentative assignment of several resonances to a specific lysine in the sequence. Molla A, Kilhoffer MC, Ferraz C, Audemard E, Walsh MP, Demaille JG (1981) Octopus calmodulin. The trimethyllysyl residue is not required for myosin light chain kinase activation. The Journal of biological chemistry 256, 15-18 [PubMed:6450198] [show Abstract] Octopus calmodulin was purified to homogeneity and shown to contain 0.1 residue each of epsilon-N-monomethyl-lysine, epsilon-N-dimethyllysine, and epsilon-N-trimethyllysine/mol. With the exception of this partial methylation and of a single tyrosyl residue, it shared all the characteristic properties of mammalian calmodulin in terms of molecular weight, amino acid composition, electrophoretic behavior in the presence or absence of Ca2+ ions, and activation of calcium/calmodulin-dependent myosin light chain kinase. In fact, Octopus calmodulin proved to be slightly more effective than ram testis calmodulin in activating both skeletal and smooth muscle myosin light chain kinases in the presence of Ca2+. This provides conclusive evidence that (a) stoichiometric trimethylation of lysine 115 is not required for enzyme activation, and (b) the inability of troponin C to activate myosin light chain kinase (Walsh, M. P., Vallet, B., Cavadore, J. C., and Demaille, J. G. Weihing RR, Korn ED (1970) Epsilon-N-dimethyllysine in amoeba actin. Nature 227, 1263-1264 [PubMed:5212577] Last Modified 16 December 2014