EC 3.5.1.114 - N-acyl-aromatic-L-amino acid amidohydrolase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 3.5.1.114

Names

Accepted name:
N-acyl-aromatic-L-amino acid amidohydrolase
Other names:
aminoacylase 3
aminoacylase III
ACY3 (gene name)
Systematic name:
N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

Reactions

Cofactor

Comments:

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 Nα-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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Pushkin, A., Carpenito, G., Abuladze, N., Newman, D., Tsuprun, V., Ryazantsev, S., Motemoturu, S., Sassani, P., Solovieva, N., Dukkipati, R., Kurtz, I.
    Structural characterization, tissue distribution, and functional expression of murine aminoacylase III.
    Am. J. Physiol., Cell Physiol. 286: C848-C856 (2004). [PMID: 14656720]
  2. Newman, D., Abuladze, N., Scholz, K., Dekant, W., Tsuprun, V., Ryazantsev, S., Bondar, G., Sassani, P., Kurtz, I., Pushkin, A.
    Specificity of aminoacylase III-mediated deacetylation of mercapturic acids.
    Drug Metab. Dispos. 35: 43-50 (2007). [PMID: 17012540]
  3. Tsirulnikov, K., Abuladze, N., Newman, D., Ryazantsev, S., Wolak, T., Magilnick, N., Koag, M. C., Kurtz, I., Pushkin, A.
    Mouse aminoacylase 3: a metalloenzyme activated by cobalt and nickel.
    Biochim. Biophys. Acta 1794: 1049-1057 (2009). [PMID: 19362172]
  4. Hsieh, J. M., Tsirulnikov, K., Sawaya, M. R., Magilnick, N., Abuladze, N., Kurtz, I., Abramson, J., Pushkin, A.
    Structures of aminoacylase 3 in complex with acetylated substrates.
    Proc. Natl. Acad. Sci. U.S.A. 107: 17962-17967 (2010). [PMID: 20921362]
  5. Tsirulnikov, K., Abuladze, N., Bragin, A., Faull, K., Cascio, D., Damoiseaux, R., Schibler, M. J., Pushkin, A.
    Inhibition of aminoacylase 3 protects rat brain cortex neuronal cells from the toxicity of 4-hydroxy-2-nonenal mercapturate and 4-hydroxy-2-nonenal.
    Toxicol. Appl. Pharmacol. 263: 303-314 (2012). [PMID: 22819785]

[EC 3.5.1.114 created 2013]