Acetyltransferase
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3D structure of histone acetyltransferase
An acetyltransferase (also referred to as a transacetylase) is any of a class of transferase enzymes that transfers an acetyl group in a reaction called acetylation. In biological organisms, post-translational modification of a protein via acetylation can profoundly transform its functionality by altering various properties like hydrophobicity, solubility, and surface attributes.[1] These alterations have the potential to influence the protein's conformation and its interactions with substrates, cofactors, and other macromolecules.[1]
Types of acetyltransferases
[edit]| Acetyltransferases | Substrate | Gene | Chromosome locus in humans | Gene group | Abbreviation |
| Histone acetyltransferase | Lysine residues of histones[1] | HAT1[2] | 2q31.1[2] | Lysine acetyltransferases[2] | HAT |
| Choline acetyltransferase | Choline[3] | CHAT[4] | 10q11.23[4] | NA | ChAT[3] |
| Serotonin N-acetyltransferase | Serotonin | AANAT[5] | 17q25.1[5] | GCN5-related N-acetyltransferases[5] | AANAT[5] |
| NatA acetyltransferase | N-terminus of various proteins as they emerge from the ribosome | NAA15[6] | 4q31.1[6] | Armadillo-like helical domain containing N-alpha-acetyltransferase subunits[6] | NatA[6] |
| NatB acetyltransferase | Peptides starting with Met-Asp/Glu/Asn/Gln[7] | NAA25[8] | 12q24.13[8] | N-alpha-acetyltransferase subunits of
microRNA protein-coding host genes[8] |
NatB[8] |
Additional examples of acetyltransferases found in nature include:
Structure
[edit]The predicted three-dimensional structures of histone, choline, and serotonin acetyltransferases are shown below.[citation needed] As with all enzymes, the structures of acetyltransferases are essential for interactions between them and their substrates; alterations to the structures of these enzymes often result in a loss of enzymatic activity.
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3D structure of histone acetyltransferase
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3D Structure of choline acetyltransferase -
3D structure of serotonin N-acetyltransferase
See also
[edit]References
[edit]- ^ a b c Marmorstein R, Zhou MM (July 2014). "Writers and readers of histone acetylation: structure, mechanism, and inhibition". Cold Spring Harbor Perspectives in Biology. 6 (7): a018762. doi:10.1101/cshperspect.a018762. PMC 4067988. PMID 24984779.
- ^ a b c Verreault A, Kaufman PD, Kobayashi R, Stillman B (January 1998). "Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase". Current Biology. 8 (2): 96–108. doi:10.1016/s0960-9822(98)70040-5. PMID 9427644. S2CID 201273.
- ^ a b Kim AR, Rylett RJ, Shilton BH (December 2006). "Substrate binding and catalytic mechanism of human choline acetyltransferase". Biochemistry. 45 (49): 14621–14631. doi:10.1021/bi061536l. PMID 17144655.
- ^ a b Strauss WL, Kemper RR, Jayakar P, Kong CF, Hersh LB, Hilt DC, Rabin M (February 1991). "Human choline acetyltransferase gene maps to region 10q11-q22.2 by in situ hybridization". Genomics. 9 (2): 396–398. doi:10.1016/0888-7543(91)90273-H. PMID 1840566.
- ^ a b c d Coon SL, Mazuruk K, Bernard M, Roseboom PH, Klein DC, Rodriguez IR (May 1996). "The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression". Genomics. 34 (1): 76–84. doi:10.1006/geno.1996.0243. PMID 8661026.
- ^ a b c d Arnesen T, Van Damme P, Polevoda B, Helsens K, Evjenth R, Colaert N, et al. (May 2009). "Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans". Proceedings of the National Academy of Sciences of the United States of America. 106 (20): 8157–8162. Bibcode:2009PNAS..106.8157A. doi:10.1073/pnas.0901931106. PMC 2688859. PMID 19420222.
- ^ Hong H, Cai Y, Zhang S, Ding H, Wang H, Han A (April 2017). "Molecular Basis of Substrate Specific Acetylation by N-Terminal Acetyltransferase NatB". Structure. 25 (4): 641–649.e3. doi:10.1016/j.str.2017.03.003. PMID 28380339.
- ^ a b c d Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, et al. (July 2012). "N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB". Proceedings of the National Academy of Sciences of the United States of America. 109 (31): 12449–12454. Bibcode:2012PNAS..10912449V. doi:10.1073/pnas.1210303109. PMC 3412031. PMID 22814378.
External links
[edit]- Acetyltransferases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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