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FEBS Lett. 2007 May 1;581(9):1898-902. Epub 2007 Apr 9.

Structural characterization of dimeric murine aminoacylase III.

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Department of Biological Chemistry, David Geffen School of Medicine, University of California at Los Angeles, Room 33-080 CHS, 10833 Le Conte Avenue, CA 90095-1689, USA.


Aminoacylase III (AAIII) plays an important role in deacetylation of acetylated amino acids and N-acetylated S-cysteine conjugates of halogenated alkenes and alkanes. AAIII, recently cloned from mouse kidney and partially characterized, is a mixture of tetramers and dimers. In the present work, AAIII dimers were purified and shown to be enzymatically active. Limited trypsinolysis showed two domains of approximately 9 and 25 kDa. The three-dimensional structure of the dimer was studied by electron microscopy of negative stained samples and by single-particle reconstruction. A 16A resolution model of the AAIII dimer was created. It has an unusual, cage-like, structure. A realistic AAIII tetramer model was built from two dimers.

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