Acetyltransferase

Class of enzymes From Wikipedia, the free encyclopedia

An acetyltransferase (also referred to as a transacetylase) is any of a class of transferase enzymes that transfers an acetyl group in a reaction 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 locus in humans Gene group Abbreviation
Histone acetyltransferase Lysine residues of 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 of

microRNA protein-coding host genes[8]

NatB[8]

Additional examples of acetyltransferases found in nature include:

Structure

The predicted three-dimensional structures of histone, choline, and serotonin acetyltransferases are shown below.[citation needed] As with all enzymes, the structures of acetyltransferases are essential for interactions between them and their substrates; alterations to the structures of these enzymes often result in a loss of enzymatic activity.

See also

References

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