changed by alanine (A) is a strong reduction in the acetyltransferase activity. Moreover, there are a series of mutations which cause a reduction of the protein activity. These are: The substitution of phenylalanine (F) by alanine (A) in the 105th position. The substitution of valine (v) by alanine (A) in the 106th position. Leucine (L) by alanine (A) in the 107th position. Aspartic acid (D) by alanine (A) in the 108th position. Glutamic acid (E) by alanine (A) in the 115th and 117th position. In some cases, this reduction of activity is even stronger such as in the following mutations: Asparagine (N) by alanine (A) in the 182nd position. Phenylalanine (F) by alanine (A) in the 183th position. There are some mutations which lead to an increase of activity such as: Aspartic acid (D) by alanine (A) in the 109th position Aspartic acid (D) by arginine (R) in the 109th position. It is important to mention that this increase in activity is generally a marginal event. Glutamic acid (E) by alanine (A) in the 111th position. In this case, the increase of activity is regarding the 2-fold. There are some cases in which the mutation of the gene might cause a reduction in the acetylation of the microtubules. Like for example: Cysteine (C) by alanine (A) in the 120th position. Aspartic acid (D) by glutamic acid (E) in the 157th position. Nevertheless, not always a mutation due to a substitution of one aminoacid by another one has a particular effect on the activity of the protein. There are some examples in which a mutation doesn't produce a significant variation of the catalytic effect of the protein. These are: Serine (S) by alanine (A) in the 61st position. Glutamic acid (E) by arginine (R) in the 111th position. Post Translational Modifications ATAT1 suffers post translational modifications, which are changes in the protein after it has been translated by ribosomes. The amino acids generally affected by these modifications are in position 46, 146, 233, 244, 272, 276, 315. The main effect of this modifications is an increase in the acetylation of tubulin. Associated diseases Knockout studies of the mouse enzymes have shown new possible biological functions. Therefore, they have shown some associated diseases, as well. For example, abnormal levels of acetylation are closely linked to neurological disorders, cancer, heart diseases and other illnesses. For some of these diseases a possible solution is