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Acetyltransferase

From Wikipedia, the free encyclopedia

An acetyltransferase (also referred to as a transacetylase) is a type of transferase enzyme that transfers an acetyl group, through a process 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

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Table 1: Types of acetyltransferases found in humans
Acetyltransferases Substrate Gene Chromosome Location Gene Group Abbreviation
Histone Acetyltransferase Lysine residues on 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

MicroRNA protein coding host genes[8]

NatB[8]

Additional examples of acetyltransferases found in nature include:

Structure

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The predicted three-dimensional structures of histone, choline, and serotonin acetyltransferases are shown below.[citation needed] As with all enzymes, the structure of acetyltransferases are essential for interactions between them and their substrates; alterations to the structures of these enzymes could result in a loss of enzymatic activity.

See also

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References

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  1. ^ 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.
  2. ^ 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.
  3. ^ 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.
  4. ^ 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.
  5. ^ 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.
  6. ^ 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.
  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. ^ 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.
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