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1-Butaneboronic Acid Binding to Aeromonas proteolytica Aminopeptidase:  A Case of Arrested Development
  • Carin C. De Paola, Brandeis University
  • Brian Bennett, Marquette University
  • Richard C. Holz, Marquette University
  • Dagmar Ringe, Brandeis University
  • Gregory A. Petsko, Brandeis University
Document Type
Format of Original
6 p.
Publication Date
American Chemical Society
Original Item ID
doi: 10.1021/bi9900572
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.

Biochemistry, Vol. 38, No. 28 (July 1999): 9048-9053. DOI.

Brian Bennett and Richard Holz were affiliated with Utah State University at the time of publication.

Citation Information
Carin C. De Paola, Brian Bennett, Richard C. Holz, Dagmar Ringe, et al.. "1-Butaneboronic Acid Binding to Aeromonas proteolytica Aminopeptidase:  A Case of Arrested Development" Biochemistry (1999) ISSN: 0006-2960
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