| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2050165 | FEBS Letters | 2007 | 5 Pages |
Abstract
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 ∼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 16 Å 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.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Sergey Ryazantsev, Natalia Abuladze, Debra Newman, Galyna Bondar, Ira Kurtz, Alexander Pushkin,