1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development. Academic Article uri icon

Overview

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 A 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.

publication date

  • July 13, 1999

Research

keywords

  • Aeromonas
  • Aminopeptidases
  • Boron Compounds
  • Enzyme Inhibitors

Identity

Scopus Document Identifier

  • 0033551445

Digital Object Identifier (DOI)

  • 10.1021/bi9900572

PubMed ID

  • 10413478

Additional Document Info

volume

  • 38

issue

  • 28