The zinc metalloproteases are a diverse group of enzymes which are becoming increasingly important in a variety of biological systems. Their major function is to break down proteins. This text presents recent research results on the biochemistry and molecular biology of these enzymes.
Table of Contents
The biological importance of zinc and families of zinc metalloproteases, Nigel M. Hooper; astacin family of metalloendopeptidases, Judith S. Bond and Weiping Jiang; the reprolysins - a family of metalloproteinases defined by snake venom and mammalian metalloproteinases, Jay W. Fox and Jon B. Bjarnason; biochemical, molecular and genetic aspects of angiotensin I-converting enzyme, Tracy A. Williams et al; neutral endopeptidase-24.11 - structure, and design and clinical use of inhibitors, Ann Beaumont et al; aminopeptidases - structure and biological function, Jiyang Wang and Max D. Cooper; matrix metalloproteinases - Hideaki Nagase; tetanus and botulism neurotoxins, Giampietro Schiavo et al; insulin degrading enzyme - a new type of metalloprotease, William C. Duckworth and Frederick G. Hamel; structure and function of mammalian zinc carboxypeptidases, R.A. Skidgel; molecular and functional aspects of membrane didpeptidase, S. Keynan et al; endothelin-converting enzyme - structure and localization, Anthony J. Turner and Kazuhiko Tanzawa.