FEBS letters, 2007-05, Vol.581 (9), p.1898-1902
2007
Volltextzugriff (PDF)
Details
- Autor(en) / Beteiligte
- Titel
- Structural characterization of dimeric murine aminoacylase III
- Ist Teil von
- FEBS letters, 2007-05, Vol.581 (9), p.1898-1902
- Ort / Verlag
- England: Elsevier B.V
- Erscheinungsjahr
- 2007
- Quelle
- Wiley Online Library Journals Frontfile Complete
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0014-5793eISSN: 1873-3468DOI: 10.1016/j.febslet.2007.03.088Titel-ID: cdi_proquest_miscellaneous_70412634
- Format
- –
- Schlagworte
- 3D reconstruction, Amidohydrolases - chemistry, Amidohydrolases - isolation & purification, Amidohydrolases - metabolism, Animals, Catalysis, Deacetylation, Dimerization, Electron microscopy, Imaging, Three-Dimensional, Kidney, Mice, Microscopy, Electron, Models, Molecular, Murine aminoacylase III, Trypsin - metabolism