| First Author | Ryazantsev S | Year | 2007 |
| Journal | FEBS Lett | Volume | 581 |
| Issue | 9 | Pages | 1898-902 |
| PubMed ID | 17434493 | Mgi Jnum | J:121414 |
| Mgi Id | MGI:3710020 | Doi | 10.1016/j.febslet.2007.03.088 |
| Citation | Ryazantsev S, et al. (2007) Structural characterization of dimeric murine aminoacylase III. FEBS Lett 581(9):1898-902 |
| abstractText | 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. |
