1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development. Biochemistry 1999 Jul 13;38(28):9048-53
Date
07/22/1999Pubmed ID
10413478DOI
10.1021/bi9900572Scopus ID
2-s2.0-0033551445 (requires institutional sign-in at Scopus site) 46 CitationsAbstract
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.
Author List
De Paola CC, Bennett B, Holz RC, Ringe D, Petsko GAAuthor
Brian Bennett D.Phil. Professor and Chair in the Physics department at Marquette UniversityMESH terms used to index this publication - Major topics in bold
AeromonasAminopeptidases
Animals
Binding, Competitive
Boron Compounds
Catalysis
Cattle
Crystallization
Crystallography, X-Ray
Enzyme Inhibitors
Hydrolysis
Lens, Crystalline
Leucyl Aminopeptidase
Models, Molecular
Protein Conformation
Spectrophotometry
Substrate Specificity
Zinc
