Acetyltransferase (or transacetylase) is a type of transferaseenzyme that transfers an acetyl group, through a process called acetylation. Acetylation serves as a modification that can profoundly transform the functionality of a protein by modifying 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] The image to the right shows the basic structure of an acetyl group, where R is a variable indicates the remainder of the molecule to which the acetyl group is attached.
Chemical structure of an acetyl group bound to the remainder R of a molecule.
Table 1: Classification of acetyltransferases in human
The 3D structure predictions of histone, choline, and serotonin acetyltransferases are shown to the side of this page. The 3D structure of these proteins are essential for interactions between them and their substrates. Alterations to the 3D structures of these enzymes could result in the chemical modifications not being completed.
^ abcMarmorstein 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. PMC4067988. PMID 24984779.
^ abcVerreault 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.
^ abKim 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.
^ abStrauss 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.
^ abcdCoon 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.
^ abcdArnesen 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. PMC2688859. 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.
^ abcdVan 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. PMC3412031. PMID 22814378.
acetyltransferase, transacetylase, type, transferase, enzyme, that, transfers, acetyl, group, through, process, called, acetylation, acetylation, serves, modification, that, profoundly, transform, functionality, protein, modifying, various, properties, like, h. Acetyltransferase or transacetylase is a type of transferase enzyme that transfers an acetyl group through a process called acetylation Acetylation serves as a modification that can profoundly transform the functionality of a protein by modifying 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 The image to the right shows the basic structure of an acetyl group where R is a variable indicates the remainder of the molecule to which the acetyl group is attached Chemical structure of an acetyl group bound to the remainder R of a molecule Table 1 Classification of acetyltransferases in human 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 Contents 1 Structure 2 See also 3 References 4 External linksStructure edit nbsp 3D structure of histone acetyltransferase nbsp 3D Structure of choline acetyltransferase nbsp 3D structure of serotonin N acetyltransferase The 3D structure predictions of histone choline and serotonin acetyltransferases are shown to the side of this page The 3D structure of these proteins are essential for interactions between them and their substrates Alterations to the 3D structures of these enzymes could result in the chemical modifications not being completed Additional examples include Chloramphenicol acetyltransferaseSee also editAcyltransferase AcetylationReferences 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 editAcetyltransferases at the U S National Library of Medicine Medical Subject Headings MeSH nbsp This enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Acetyltransferase amp oldid 1189880906, wikipedia, wiki, book, books, library,
