Title

1-Butaneboronic Acid Binding to Aeromonas proteolytica Aminopeptidase:  A Case of Arrested Development

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.

Comments

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.