This enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It preferentially deacetylates Nalpha-acetylated aromatic amino acids and mercapturic acids (S-conjugates of N-acetyl-L-cysteine) that are usually not deacetylated by EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase. The enzyme is significantly activated by Co2+ and Ni2+ . Some bacterial aminoacylases demonstrate substrate specificity for both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase and EC 3.5.1.15, aspartoacylase.
This enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It preferentially deacetylates Nalpha-acetylated aromatic amino acids and mercapturic acids (S-conjugates of N-acetyl-L-cysteine) that are usually not deacetylated by EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase. The enzyme is significantly activated by Co2+ and Ni2+ [3]. Some bacterial aminoacylases demonstrate substrate specificity for both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase and EC 3.5.1.15, aspartoacylase.
the 90000-100000 Da AA3 form (that is detected in most hepatocellular carcinoma cell lines but not in normal hepatocytes) is functionally active and together with the normal 35000 Da AA3 form mediates the deacetylation of N-acetylfarnesylcysteine and N-acetylgeranylgeranylcysteine
the 90000-100000 Da AA3 form (that is detected in most hepatocellular carcinoma cell lines but not in normal hepatocytes) is functionally active and together with the normal 35000 Da AA3 form mediates the deacetylation of N-acetylfarnesylcysteine and N-acetylgeranylgeranylcysteine
the 90000-100000 Da AA3 form (that is detected in most hepatocellular carcinoma cell lines but not in normal hepatocytes) is functionally active and together with the normal 35000 Da AA3 form mediates the deacetylation of N-acetylfarnesylcysteine and N-acetylgeranylgeranylcysteine
the 90000-100000 Da AA3 form (that is detected in most hepatocellular carcinoma cell lines but not in normal hepatocytes) is functionally active and together with the normal 35000 Da AA3 form mediates the deacetylation of N-acetylfarnesylcysteine and N-acetylgeranylgeranylcysteine
aminoacylase 3 inhibition completely protects rat brain cortex neurons expressing the enzyme from the toxicity of 4-hydroxy-2-nonenal-mercapturate. 4-hydroxy-2-nonenal-cysteine is also neurotoxic and its toxicity is mostly prevented by a beta-lyase inhibitor, aminooxyacetate
the enzyme cleaves the conjugates 4-hydroxy-2-nonenal mercapturate and acrolein mercapturate formed by reaction with glutathione for detoxification in the GSH-conjugation pathway, overview. Aminoacylase 3 is involved in the neurotoxicity of the compounds 4-hydroxy-2-nonenal and acrolein
expression is significantly elevated in the livers of hepatocellular carcinoma patients and hepatocellular carcinoma cell lines. Treatment of HepG2 cells with AA3 inhibitors, and HepG2 and HuH7 with AA3 siRNA significantly decreases Ras membrane association and is toxic to these HCC cell lines. AA3 inhibition may be an effective approach in the therapy of hepatocellular carcinoma and elevated AA3 expression in hepatocellular carcinoma is potentially an important diagnostic marker