Acetiltransferase

Unha acetiltransferase (ou transacetilase) é un tipo de encima transferase que transfire un grupo acetilo, nun proceso chamado acetilación. A acetilación serve para crear unha modificación que pode transformar profundamente a funcionalidade dunha molécula, como unha proteína, ao modificar varias propoedades como a hidrofobicidade, solubilidade e atributos de superficie.^[1] Estas alteracións poden influír na conformación da proteína e na súa interacción cos substratos, cofactores e outras macromoléculas.^[1]

Táboa 1: Exemplos de acetiltransferases
Acetiltransferases	Substrato	Xene	Localización cromosómica	Grupo xénico	Abreviatura
Histona acetiltransferase	Residuos de lisina en histonas^[1]	HAT1^[2]	2q31.1^[2]	Lisina acetiltransferases^[2]	HAT
Colina acetiltransferase	Colina^[3]	CHAT^[4]	10q11.23^[4]		ChAT^[3]
Serotonina N-acetiltransferase	Serotonina	AANAT^[5]	17q25.1^[5]	N-Acetiltransferases relacionadas con GCN5^[5]	AANAT^[5]
NatA acetiltransferase	N-terminal de varias proteínas a medida que sae do ribosoma	NAA15^[6]	4q31.1^[6]	Dominio helicoidal similar ao Armadillo Contén subunidades de N-alfa-acetiltransferase^[6]	NatA^[6]
NatB acetiltransferase	Péptidos que empezan con Met-Asp/Glu/Asn/Gln^[7]	NAA25^[8]	12q24.13^[8]	Subunidades de N-alfa-acetiltransferase^[8]	NatB^[8]

Estrutura

Estrutura en 3D da histona acetiltransferase
Estrutura en 3D da colina acetiltransferase
Estrutura en 3D da serotonina N-acetiltransferase

As predicións da estrutura tridimensional das histona-, colina-, e serotonina acetiltransferases móstranse nas imaxes.

Outro exemplo, neste caso dunha acetiltransferase bacteriana, é a cloranfenicol acetiltransferase, que detoxifica o antibiótico cloranfenicol e dálle á bacteria resistencia ao cloranfenicol.

Notas

↑ ^1,0 ^1,1 ^1,2 Marmorstein R, Zhou MM (xullo de 2014). "Writers and readers of histone acetylation: structure, mechanism, and inhibition". Cold Spring Harbor Perspectives in Biology 6 (7): a018762. PMC 4067988. PMID 24984779. doi:10.1101/cshperspect.a018762.
↑ ^2,0 ^2,1 ^2,2 Verreault A, Kaufman PD, Kobayashi R, Stillman B (xaneiro de 1998). "Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase". Current Biology 8 (2): 96–108. PMID 9427644. doi:10.1016/s0960-9822(98)70040-5.
↑ ^3,0 ^3,1 Kim AR, Rylett RJ, Shilton BH (decembro de 2006). "Substrate binding and catalytic mechanism of human choline acetyltransferase". Biochemistry 45 (49): 14621–14631. PMID 17144655. doi:10.1021/bi061536l.
↑ ^4,0 ^4,1 Strauss WL, Kemper RR, Jayakar P, Kong CF, Hersh LB, Hilt DC, Rabin M (febreiro de 1991). "Human choline acetyltransferase gene maps to region 10q11-q22.2 by in situ hybridization". Genomics 9 (2): 396–398. PMID 1840566. doi:10.1016/0888-7543(91)90273-H.
↑ ^5,0 ^5,1 ^5,2 ^5,3 Coon SL, Mazuruk K, Bernard M, Roseboom PH, Klein DC, Rodriguez IR (maio de 1996). "The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression". Genomics 34 (1): 76–84. PMID 8661026. doi:10.1006/geno.1996.0243.
↑ ^6,0 ^6,1 ^6,2 ^6,3 Arnesen T, Van Damme P, Polevoda B, Helsens K, Evjenth R, Colaert N, et al. (maio de 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. PMC 2688859. PMID 19420222. doi:10.1073/pnas.0901931106.
↑ Hong H, Cai Y, Zhang S, Ding H, Wang H, Han A (abril de 2017). "Molecular Basis of Substrate Specific Acetylation by N-Terminal Acetyltransferase NatB". Structure 25 (4): 641–649.e3. PMID 28380339. doi:10.1016/j.str.2017.03.003.
↑ ^8,0 ^8,1 ^8,2 ^8,3 Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, et al. (xullo de 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. PMC 3412031. PMID 22814378. doi:10.1073/pnas.1210303109.

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Ligazóns externas

Acetyltransferases Medical Subject Headings (MeSH) na Biblioteca Nacional de Medicina dos EUA.

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[:0-1] 1,0 ^1,1 ^1,2 Marmorstein R, Zhou MM (xullo de 2014). "Writers and readers of histone acetylation: structure, mechanism, and inhibition". Cold Spring Harbor Perspectives in Biology 6 (7): a018762. PMC 4067988. PMID 24984779. doi:10.1101/cshperspect.a018762.

[:1-2] 2,0 ^2,1 ^2,2 Verreault A, Kaufman PD, Kobayashi R, Stillman B (xaneiro de 1998). "Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase". Current Biology 8 (2): 96–108. PMID 9427644. doi:10.1016/s0960-9822(98)70040-5.

[:2-3] 3,0 ^3,1 Kim AR, Rylett RJ, Shilton BH (decembro de 2006). "Substrate binding and catalytic mechanism of human choline acetyltransferase". Biochemistry 45 (49): 14621–14631. PMID 17144655. doi:10.1021/bi061536l.

[:3-4] 4,0 ^4,1 Strauss WL, Kemper RR, Jayakar P, Kong CF, Hersh LB, Hilt DC, Rabin M (febreiro de 1991). "Human choline acetyltransferase gene maps to region 10q11-q22.2 by in situ hybridization". Genomics 9 (2): 396–398. PMID 1840566. doi:10.1016/0888-7543(91)90273-H.

[:4-5] 5,0 ^5,1 ^5,2 ^5,3 Coon SL, Mazuruk K, Bernard M, Roseboom PH, Klein DC, Rodriguez IR (maio de 1996). "The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression". Genomics 34 (1): 76–84. PMID 8661026. doi:10.1006/geno.1996.0243.

[:5-6] 6,0 ^6,1 ^6,2 ^6,3 Arnesen T, Van Damme P, Polevoda B, Helsens K, Evjenth R, Colaert N, et al. (maio de 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. PMC 2688859. PMID 19420222. doi:10.1073/pnas.0901931106.

[7] Hong H, Cai Y, Zhang S, Ding H, Wang H, Han A (abril de 2017). "Molecular Basis of Substrate Specific Acetylation by N-Terminal Acetyltransferase NatB". Structure 25 (4): 641–649.e3. PMID 28380339. doi:10.1016/j.str.2017.03.003.

[:6-8] 8,0 ^8,1 ^8,2 ^8,3 Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, et al. (xullo de 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. PMC 3412031. PMID 22814378. doi:10.1073/pnas.1210303109.

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