Structural characterization of dimeric murine aminoacylase III.
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.
Ryazantsev
Sergey
S
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.
Abuladze
Natalia
N
Newman
Debra
D
Bondar
Galyna
G
Kurtz
Ira
I
Pushkin
Alexander
A
D000581:Amidohydrolases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D019281:Dimerization; D021621:Imaging, Three-Dimensional; D051379:Mice; D008854:Microscopy, Electron; D008958:Models, Molecular; D014357:Trypsin / Q000378:metabolism
D014357:Trypsin; D000581:Amidohydrolases; C483737:aminoacylase III, mouse