Acetyltransferase

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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]

Contents

Types of acetyltransferases

Table 1: Types of acetyltransferases found in humans
AcetyltransferasesSubstrateGeneChromosome locus in humansGene groupAbbreviation
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] NAChAT [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 ribosomeNAA15 [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

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.

See also

References

  1. 1 2 3 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.
  2. 1 2 3 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. Bibcode:1998CBio....8...96V. doi: 10.1016/s0960-9822(98)70040-5 . PMID   9427644. S2CID   201273.
  3. 1 2 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.
  4. 1 2 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.
  5. 1 2 3 4 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.
  6. 1 2 3 4 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.
  7. ↑ 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.
  8. 1 2 3 4 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.
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