User:Jlp21k/Acetyltransferase: Difference between revisions
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[[File:Acetyl.svg|thumb|Chemical structure of an acetyl group bound to the remainder R of a molecule.]] |
[[File:Acetyl.svg|thumb|Chemical structure of an acetyl group bound to the remainder R of a molecule.]] |
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'''Acetyltransferase''' (or '''transacetylase''') is a type of [[transferase]] [[enzyme]] that transfers an [[acetyl]] group, 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. These alterations have the potential to influence the protein's conformation and its interactions with substrates, cofactors, and other macromolecules. |
'''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. These alterations have the potential to influence the protein's conformation and its interactions with substrates, cofactors, and other macromolecules. |
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|+Table 1: Classification of acetyltransferases in human |
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|'''Acetyltransferases''' |
|'''Acetyltransferases''' |
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|'''Substrate''' |
|'''Substrate''' |
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Revision as of 12:53, 18 November 2023
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. These alterations have the potential to influence the protein's conformation and its interactions with substrates, cofactors, and other macromolecules.
| Acetyltransferases | Substrate | Gene (Human) | Chromosome Location (Human) | Gene Group | Abbreviation |
| Histone Acetyltransferase | Lysine residues on histones1 | HAT12 | 2q31.12 | Lysine acetyltransferases2 | HAT |
| Choline Acetyltransferase | Choline3 | CHAT4 | 10q11.234 | NA | ChAT3 |
| Serotonin N-Acetyltransferase | Serotonin | AANAT5 | 17q25.15 | GCN5 Related N-Acetyltransferases5 | AANAT5 |
| NatA Acetyltransferase | N-terminus of various proteins as they emerge from the ribosome | NAA156 | 4q31.16 | Armadillo like helical domain containing
N-alpha-acetyltransferase subunits6 |
NatA6 |
| NatB Acetyltransferase | Peptides starting with Met-Asp/Glu/Asn/Gln8 | NAA257 | 12q24.137 | N-alpha-acetyltransferase subunits
MicroRNA protein coding host genes7 |
NatB7 |
Additional examples include:
See also
External links
- Acetyltransferases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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References
1. Marmorstein R, Zhou MM. Writers and readers of histone acetylation: structure, mechanism, and inhibition. Cold Spring Harb Perspect Biol. 2014 Jul 1;6(7):a018762. doi: 10.1101/cshperspect.a018762. PMID: 24984779; PMCID: PMC4067988.
2. Verreault, A., Kaufman, P. D., Kobayashi, R., & Stillman, B. (1998). Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase. ''Current biology : CB'', ''8''(2), 96–108. <nowiki>https://doi.org/10.1016/s0960-9822(98)70040-5</nowiki>
3. Kim, A. R., Rylett, R. J., & Shilton, B. H. (2006). Substrate binding and catalytic mechanism of human choline acetyltransferase. ''Biochemistry'', ''45''(49), 14621–14631. <nowiki>https://doi.org/10.1021/bi061536l</nowiki>
4. Strauss, W. L., Kemper, R. R., Jayakar, P., Kong, C. F., Hersh, L. B., Hilt, D. C., & Rabin, M. (1991). Human choline acetyltransferase gene maps to region 10q11-q22.2 by in situ hybridization. ''Genomics'', ''9''(2), 396–398. <nowiki>https://doi.org/10.1016/0888-7543(91)90273-h</nowiki>
5. Coon, S. L., Mazuruk, K., Bernard, M., Roseboom, P. H., Klein, D. C., & Rodriguez, I. R. (1996). The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression. ''Genomics'', ''34''(1), 76–84. <nowiki>https://doi.org/10.1006/geno.1996.0243</nowiki>
6. Arnesen, T., Van Damme, P., Polevoda, B., Helsens, K., Evjenth, R., Colaert, N., Varhaug, J. E., Vandekerckhove, J., Lillehaug, J. R., Sherman, F., & Gevaert, K. (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. <nowiki>https://doi.org/10.1073/pnas.0901931106</nowiki>
7. Van Damme, P., Lasa, M., Polevoda, B., Gazquez, C., Elosegui-Artola, A., Kim, D. S., De Juan-Pardo, E., Demeyer, K., Hole, K., Larrea, E., Timmerman, E., Prieto, J., Arnesen, T., Sherman, F., Gevaert, K., & Aldabe, R. (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. <nowiki>https://doi.org/10.1073/pnas.1210303109</nowiki>
8. Hong, H., Cai, Y., Zhang, S., Ding, H., Wang, H., & Han, A. (2017). Molecular Basis of Substrate Specific Acetylation by N-Terminal Acetyltransferase NatB. ''Structure (London, England : 1993)'', ''25''(4), 641–649.e3.