Document Type
Article
Language
eng
Format of Original
6 p.
Publication Date
7-1999
Publisher
American Chemical Society
Source Publication
Biochemistry
Source ISSN
0006-2960
Original Item ID
doi: 10.1021/bi9900572
Abstract
Hydrolases containing two metal ions connected by a bridging ligand catalyze reactions important in carcinogensis, tissue repair, post-translational modification, control and regulation of biochemical pathways, and protein degradation. The aminopeptidase from Aeromonas proteolytica serves as a paradigm for the study of such bridged bimetallic proteases since its three-dimensional structure is known to very high resolution and its catalytic reaction is amenable to spectroscopic examination. Herein, we report the X-ray crystal structure at 1.9 Å resolution of AAP complexed with 1-butaneboronic acid (BuBA). This structure suggests that this complex represents a snapshot of the proteolytic reaction in an arrested form between the Michaelis complex and the transition state. Comparison of the structure with spectroscopic and other data allows us to conclude that the apparently structurally symmetrical dizinc site is actually asymmetric electrostatically.
Recommended Citation
De Paola, Carin C.; Bennett, Brian; Holz, Richard C.; Ringe, Dagmar; and Petsko, Gregory A., "1-Butaneboronic Acid Binding to Aeromonas proteolytica Aminopeptidase: A Case of Arrested Development" (1999). Physics Faculty Research and Publications. 52.
https://epublications.marquette.edu/physics_fac/52
Comments
Accepted version. Biochemistry, Vol. 38, No. 28 (July 1999): 9048-9053. DOI. © 1999 American Chemical Society Publications. Used with permission.
Brian Bennett and Richard Holz were affiliated with Utah State University at the time of publication.