Acetyltransferase

3D structure of histone acetyltransferase

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

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:

Chloramphenicol acetyltransferase

Structure

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.

3D structure of histone acetyltransferase
3D Structure of choline acetyltransferase
3D structure of serotonin N-acetyltransferase

References

^ ^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

Acetyltransferases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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[:0-1] 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.

[:1-2] 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.

[:2-3] 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.

[:3-4] 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.

[:4-5] 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.

[:5-6] 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.

[:6-8] 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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v t e Transferases: acyltransferases (EC 2.3)
2.3.1: other than amino-acyl groups	acetyltransferases: Acetyl-Coenzyme A acetyltransferase N-Acetylglutamate synthase Choline acetyltransferase Dihydrolipoyl transacetylase Acetyl-CoA C-acyltransferase Beta-galactoside transacetylase Chloramphenicol acetyltransferase N-acetyltransferase Serotonin N-acetyl transferase HGSNAT ARD1A Histone acetyltransferase P300/CBP NAT2 palmitoyltransferases: Carnitine O-palmitoyltransferase CPT1 CPT2 Serine C-palmitoyltransferase SPTLC1 SPTLC2 other: Acyltransferase like 2 Aminolevulinic acid synthase Beta-ketoacyl-ACP synthase Glyceronephosphate O-acyltransferase Lecithin—cholesterol acyltransferase Glycerol-3-phosphate O-acyltransferase 1-acylglycerol-3-phosphate O-acyltransferase 2-acylglycerol-3-phosphate O-acyltransferase ABHD5
2.3.2: Aminoacyltransferases	Gamma-glutamyl transpeptidase Peptidyl transferase Transglutaminase Tissue transglutaminase Keratinocyte transglutaminase Factor XIII
2.3.3: converted into alkyl on transfer	Citrate synthase Decylcitrate synthase Citrate (Re)-synthase Decylhomocitrate synthase 2-methylcitrate synthase 2-ethylmalate synthase 3-ethylmalate synthase ATP citrate lyase Malate synthase HMG-CoA synthase HMGCS2 2-hydroxyglutarate synthase 3-propylmalate synthase 2-isopropylmalate synthase Homocitrate synthase Sulfoacetaldehyde acetyltransferase

Acetyltransferase

Types of acetyltransferases

Structure

See also

References

External links