Record Information |
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Version | 1.0 |
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Created at | 2005-11-16 15:48:42 UTC |
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Updated at | 2021-08-19 23:58:47 UTC |
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NP-MRD ID | NP0001103 |
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Secondary Accession Numbers | None |
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Natural Product Identification |
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Common Name | N6-Acetyl-L-lysine |
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Description | N-acetyl-lysine is an acetylated amino acid. Post-translational lysine-acetylation is one of two major modifications of lysine residues in various proteins. Acetylation of specific lysine residues in the N-terminal domains of core histones is a biochemical marker of active genes. Acetylation is now known to play a major role in eukaryotic transcription. Specifically, acetyltransferase enzymes that act on particular lysine side chains of histones and other proteins are intimately involved in transcriptional activation. By modifying chromatin proteins and transcription-related factors, these acetylases are believed to regulate the transcription of many genes. The best-characterized mechanism is acetylation, catalyzed by histone acetyltransferase (HAT) enzymes. HATs function enzymatically by transferring an acetyl group from acetyl-coenzyme A (acetyl-CoA) to the -amino group of certain lysine side chains within a histone's basic N-terminal tail region. Within a histone octamer, these regions extend out from the associated globular domains, and in the context of a nucleosome, they are believed to bind the DNA through charge interactions (positively charged histone tails associated with negatively charged DNA) or mediate interactions between nucleosomes. Lysine acetylation, which neutralizes part of a tail region's positive charge, is postulated to weaken histone-DNA or nucleosome-nucleosome interactions and/or signal a conformational change, thereby destabilizing nucleosome structure or arrangement and giving other nuclear factors, such as the transcription complex, more access to a genetic locus. In agreement with this is the fact that acetylated chromatin has long been associated with states of transcriptional activation. Specific recognition of N-acetyl-lysine is a conserved function of all bromodomains found in different proteins, recognized as an emerging intracellular signaling mechanism that plays critical roles in regulating gene transcription, cell-cycle progression, apoptosis, DNA repair, and cytoskeletal organization. (PMID 9169194 , 10827952 , 17340003 , 16247734 , 9478947 , 10839822 ). |
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Structure | CC(=O)NCCCC[C@H](N)C(O)=O InChI=1S/C8H16N2O3/c1-6(11)10-5-3-2-4-7(9)8(12)13/h7H,2-5,9H2,1H3,(H,10,11)(H,12,13)/t7-/m0/s1 |
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Synonyms | Value | Source |
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(2S)-6-(Acetylamino)-2-aminohexanoic acid | ChEBI | N(6)-ACETYLLYSINE | ChEBI | N(zeta)-Acetyllysine | ChEBI | N-epsilon-Acetyl-L-lysine | ChEBI | N-Epsilon-Acetyllysine | ChEBI | N(epsilon)-Acetyl-L-lysine | ChEBI | N(zeta)-Acetyl-L-lysine | ChEBI | (2S)-6-(Acetylamino)-2-aminohexanoate | Generator | N(Z)-Acetyllysine | Generator | N(Ζ)-acetyllysine | Generator | N(Z)-Acetyl-L-lysine | Generator | N(Ζ)-acetyl-L-lysine | Generator | e-Acetyl-L-lysine | HMDB | e-N-Acetyl-L-lysine | HMDB | e-N-Acetyllysine | HMDB | epsilon-Acetyl-L-lysine | HMDB | epsilon-N-Acetyl-L-lysine | HMDB | epsilon-N-Acetyllysine | HMDB | L-e-N-Acetyllysine | HMDB | L-epsilon-N-Acetyllysine | HMDB | N-e-Acetyl-L-lysine | HMDB | N-e-Acetyllysine | HMDB | N6-Acetyllysine | HMDB | Ne-acetyl-L-lysine | HMDB | Ne-acetyllysine | HMDB | Omega-N-acetyl-L-lysine | HMDB | W-N-Acetyl-L-lysine | HMDB | N(6)-Acetyllsine | HMDB | Omega-acetyllsine | HMDB | (2S)-6-Acetamido-2-aminohexanoic acid | HMDB | 6-Acetamido-2-aminohexanoic acid | HMDB | L-Ε-N-acetyllysine | HMDB | Nepsilon-acetyl-L-lysine | HMDB | Nepsilon-acetyllysine | HMDB | Nε-acetyl-L-lysine | HMDB | Nε-acetyllysine | HMDB | Ε-acetyl-L-lysine | HMDB | Ε-N-acetyl-L-lysine | HMDB | Ε-N-acetyllysine | HMDB | Ω-N-acetyl-L-lysine | HMDB | N6-Acetyl-L-lysine | ChEBI |
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Chemical Formula | C8H16N2O3 |
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Average Mass | 188.2242 Da |
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Monoisotopic Mass | 188.11609 Da |
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IUPAC Name | (2S)-2-amino-6-acetamidohexanoic acid |
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Traditional Name | N6-acetyllysine |
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CAS Registry Number | 692-04-6 |
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SMILES | CC(=O)NCCCC[C@H](N)C(O)=O |
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InChI Identifier | InChI=1S/C8H16N2O3/c1-6(11)10-5-3-2-4-7(9)8(12)13/h7H,2-5,9H2,1H3,(H,10,11)(H,12,13)/t7-/m0/s1 |
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InChI Key | DTERQYGMUDWYAZ-ZETCQYMHSA-N |
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Experimental Spectra |
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| Spectrum Type | Description | Depositor Email | Depositor Organization | Depositor | Deposition Date | View |
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1D NMR | 1H NMR Spectrum (1D, 500 MHz, H2O, experimental) | Wishart Lab | Wishart Lab | David Wishart | 2021-06-20 | View Spectrum | 2D NMR | [1H, 13C]-HSQC NMR Spectrum (2D, 600 MHz, H2O, experimental) | Wishart Lab | Wishart Lab | David Wishart | 2021-06-20 | View Spectrum |
| Predicted Spectra |
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| Not Available | Chemical Shift Submissions |
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| Not Available | Species |
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Species of Origin | |
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Chemical Taxonomy |
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Description | Belongs to the class of organic compounds known as l-alpha-amino acids. These are alpha amino acids which have the L-configuration of the alpha-carbon atom. |
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Kingdom | Organic compounds |
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Super Class | Organic acids and derivatives |
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Class | Carboxylic acids and derivatives |
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Sub Class | Amino acids, peptides, and analogues |
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Direct Parent | L-alpha-amino acids |
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Alternative Parents | |
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Substituents | - L-alpha-amino acid
- Medium-chain fatty acid
- Amino fatty acid
- Fatty acid
- Fatty acyl
- Amino acid
- Carboximidic acid
- Carboximidic acid derivative
- Carboxylic acid
- Monocarboxylic acid or derivatives
- Propargyl-type 1,3-dipolar organic compound
- Organic 1,3-dipolar compound
- Primary amine
- Organooxygen compound
- Organonitrogen compound
- Carbonyl group
- Primary aliphatic amine
- Organic nitrogen compound
- Organic oxygen compound
- Amine
- Organopnictogen compound
- Organic oxide
- Hydrocarbon derivative
- Aliphatic acyclic compound
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Molecular Framework | Aliphatic acyclic compounds |
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External Descriptors | |
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Physical Properties |
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State | Solid |
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Experimental Properties | |
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Predicted Properties | |
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General References | - Jacobson RH, Ladurner AG, King DS, Tjian R: Structure and function of a human TAFII250 double bromodomain module. Science. 2000 May 26;288(5470):1422-5. [PubMed:10827952 ]
- Armstrong MD, Robinow M: A case of hyperlysinemia: biochemical and clinical observations. Pediatrics. 1967 Apr;39(4):546-54. [PubMed:6022933 ]
- Crane-Robinson C, Hebbes TR, Clayton AL, Thorne AW: Chromosomal mapping of core histone acetylation by immunoselection. Methods. 1997 May;12(1):48-56. [PubMed:9169194 ]
- Jamonnak N, Fatkins DG, Wei L, Zheng W: N(epsilon)-methanesulfonyl-lysine as a non-hydrolyzable functional surrogate for N(epsilon)-acetyl-lysine. Org Biomol Chem. 2007 Mar 21;5(6):892-6. Epub 2007 Feb 5. [PubMed:17340003 ]
- Iwabata H, Yoshida M, Komatsu Y: Proteomic analysis of organ-specific post-translational lysine-acetylation and -methylation in mice by use of anti-acetyllysine and -methyllysine mouse monoclonal antibodies. Proteomics. 2005 Dec;5(18):4653-64. [PubMed:16247734 ]
- Hazen SL, d'Avignon A, Anderson MM, Hsu FF, Heinecke JW: Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Mechanistic studies identifying labile intermediates along the reaction pathway. J Biol Chem. 1998 Feb 27;273(9):4997-5005. [PubMed:9478947 ]
- Sterner DE, Berger SL: Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev. 2000 Jun;64(2):435-59. [PubMed:10839822 ]
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