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Metalloproteinases

  • Theo Hofmann
Part of the Topics in Molecular and Structural Biology book series (TMSB)

Abstract

Proteolytic enzymes are divided into four major classes on the basis of the amino acids that make up the active site and by implication confer a common mechanism on each class. The metalloproteinases constitute one of these classes, the others being the serine proteinases, the cysteine proteinases and the aspartic proteinases (formerly acid proteinases). An apparent involvement of metal ions in the action of proteinases has been shown for a large number of enzymes on the basis of activation by metal ions or of inhibition by metal-chelating agents. However, unambiguous evidence for an essential role of metal ions has been presented for only a limited number of them. To qualify as a true metalloproteinase, the metal ion should be at the ‘centre’ of the active site and be involved in the catalytic event. The only two metalloproteinases for which detailed structural and mechanistic information is available are the endoproteinase thermolysin from Bacillus thermoproteolyticus Rokko and the exoproteinase carboxypeptidase A from bovine pancreas. In this review I shall concentrate on describing recent studies on the three-dimensional structures of these enzymes and their complexes with substrate analogues and other ligands, as well as studies on their mechanism of action. Other less well characterised enzymes will be mentioned more briefly at the end. Owing to limitations of space, no attempt will be made to present a comprehensive review. For earlier studies the reader is referred to a number of reviews on the individual enzymes mentioned below.

Keywords

Peptide Bond Aspartic Proteinase Oxyanion Hole Tetrahedral Intermediate Ester Substrate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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