| First Author | Tsirulnikov K | Year | 2012 |
| Journal | FEBS Lett | Volume | 586 |
| Issue | 21 | Pages | 3799-804 |
| PubMed ID | 23010594 | Mgi Jnum | J:190334 |
| Mgi Id | MGI:5448608 | Doi | 10.1016/j.febslet.2012.09.015 |
| Citation | Tsirulnikov K, et al. (2012) Aminoacylase 3 binds to and cleaves the N-terminus of the hepatitis C virus core protein. FEBS Lett 586(21):3799-804 |
| abstractText | Aminoacylase 3 (AA3) mediates deacetylation of N-acetyl aromatic amino acids and mercapturic acids. Deacetylation of mercapturic acids of exo- and endobiotics are likely involved in their toxicity. AA3 is predominantly expressed in kidney, and to a lesser extent in liver, brain, and blood. AA3 has been recently reported to interact with the hepatitis C virus core protein (HCVCP) in the yeast two-hybrid system. Here we demonstrate that AA3 directly binds to HCVCP (K(d) ~10 muM) that may by implicated in HCV pathogenesis. AA3 also revealed a weak endopeptidase activity towards the N-terminus of HCVCP. |
