Abstract
Over the past three years, the three-dimensional structures of a number of zinc proteinases that share the zinc-binding motif HEXXHXXGXXH have been elucidated. These proteinases comprise astacin, a digestive enzyme from crayfish [1,2,3], adamalysin II [4,5] and atrolysin C [6] from snake venom, the Pseudomonas aeruginosa alkaline proteinase [7] and serralysin from Serratia marcescens proteinase [8], the collagenases from human neutrophils [9,10,11]) and fibroblasts [12,13,14,15], human stromelysin 1 [16; K. Appelt, personal communication] and matrilysin [M. Browner, Keystone Symposia, March 5–12, 1994]. These enzymes represent four different families of zinc peptidases: the astacins [3,17], the bacterial serralysins [18], the adamalysins/reprolysins [19,20], and the matrixins (matrix metalloproteinases, MMPs) [21,22].
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© 1996 Plenum Press, New York
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Bode, W. et al. (1996). The Metzincin-Superfamily of Zinc-Peptidases. In: Suzuki, K., Bond, J.S. (eds) Intracellular Protein Catabolism. Advances in Experimental Medicine and Biology, vol 389. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0335-0_1
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