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FEBS Lett. 2012 Nov 2;586(21):3799-804. doi: 10.1016/j.febslet.2012.09.015. Epub 2012 Sep 22.

Aminoacylase 3 binds to and cleaves the N-terminus of the hepatitis C virus core protein.

Author information

1
Division of Nephrology, Department of Medicine, David Geffen School of Medicine, University of California at Los Angeles, CA 90095, USA. ktsirulnikov@mednet.ucla.edu

Abstract

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 μM) that may by implicated in HCV pathogenesis. AA3 also revealed a weak endopeptidase activity towards the N-terminus of HCVCP.

PMID:
23010594
PMCID:
PMC3483449
DOI:
10.1016/j.febslet.2012.09.015
[Indexed for MEDLINE]
Free PMC Article
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