User:Jlp21k/Acetyltransferase

Chemical structure of an acetyl group bound to the remainder R of a molecule.

Acetyltransferase (or transacetylase) is a type of

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.

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]

3D structures of acetyltransferase enzymes

3D structure of histone 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 acetyltransferase

External links

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

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References

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PMID 24984779
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PMID 9427644
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ISSN 0006-2960
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ISSN 0888-7543
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ISSN 0888-7543
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PMID 19420222.{{cite journal}}: CS1 maint: PMC format (link
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PMID 28380339
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PMID 22814378.{{cite journal}}: CS1 maint: PMC format (link
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Retrieved from "https://en.wikipedia.org/w/index.php?title=User:Jlp21k/Acetyltransferase&oldid=1188766407"

[:0-1] 
PMID 24984779
.

[:1-2] 
PMID 9427644
.

[:2-3] 
ISSN 0006-2960
.

[:3-4] 
ISSN 0888-7543
.

[:4-5] 
ISSN 0888-7543
.

[:5-6] 
PMID 19420222.{{cite journal}}: CS1 maint: PMC format (link
)

[7] PMID 28380339
.

[:6-8] 
PMID 22814378.{{cite journal}}: CS1 maint: PMC format (link
)

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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