Biology: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]

Types of acetyltransferases

Table 1: Types of acetyltransferases found in humans
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

The predicted three-dimensional structures of histone, choline, and serotonin acetyltransferases are shown below. 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. ↑ 1.0 1.1 1.2 "Writers and readers of histone acetylation: structure, mechanism, and inhibition". Cold Spring Harbor Perspectives in Biology 6 (7). July 2014. doi:10.1101/cshperspect.a018762. PMID 24984779. 
  2. ↑ 2.0 2.1 2.2 "Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase". Current Biology 8 (2): 96–108. January 1998. doi:10.1016/s0960-9822(98)70040-5. PMID 9427644. Bibcode: 1998CBio....8...96V. 
  3. ↑ 3.0 3.1 "Substrate binding and catalytic mechanism of human choline acetyltransferase". Biochemistry 45 (49): 14621–14631. December 2006. doi:10.1021/bi061536l. PMID 17144655. 
  4. ↑ 4.0 4.1 "Human choline acetyltransferase gene maps to region 10q11-q22.2 by in situ hybridization". Genomics 9 (2): 396–398. February 1991. doi:10.1016/0888-7543(91)90273-H. PMID 1840566. 
  5. ↑ 5.0 5.1 5.2 5.3 "The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression". Genomics 34 (1): 76–84. May 1996. doi:10.1006/geno.1996.0243. PMID 8661026. 
  6. ↑ 6.0 6.1 6.2 6.3 "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. May 2009. doi:10.1073/pnas.0901931106. PMID 19420222. Bibcode: 2009PNAS..106.8157A. 
  7. ↑ "Molecular Basis of Substrate Specific Acetylation by N-Terminal Acetyltransferase NatB". Structure 25 (4): 641–649.e3. April 2017. doi:10.1016/j.str.2017.03.003. PMID 28380339. 
  8. ↑ 8.0 8.1 8.2 8.3 "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. July 2012. doi:10.1073/pnas.1210303109. PMID 22814378. Bibcode: 2012PNAS..10912449V. 



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