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Science 29 December 1967:
Vol. 158. no. 3809, pp. 1638 - 1644
DOI: 10.1126/science.158.3809.1638
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Articles

Evolution of Structure and Function of Proteases

Amino acid sequences of proteolytic enzymes reflect phylogenetic relationships

Hans Neurath 1, Kenneth A. Walsh 2, and William P. Winter 3

1 Department of biochemistry, University of Washington, Seattle, 98105
2 University of Washington
3 Howard Hughes Medical Institute department of biochemistry, University of Washington

One of the striking features of the proteolytic enzymes as a group is the immense variety of biological functions served by enzymes employing one of a few basic mechanisms. For example, in the higher animals, enzymes for activation of zymogens (trypsin), for digestion of dietary proteins (trypsin, chymotrypsin, elastase), for blood clotting (thrombin), for clot lysis (plasmin), and for sensing pain (kallikrein) all appear to use the same mechanism and to have evolved from the same ancestral gene by the process of gene duplication and subsequent divergent evolution. Equally striking is the variety of chemical solutions of the same functional problem, such as the peptide-bond cleavage by sulfhydryl proteases on the one hand and serine proteases on the other.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Chromosomal locations of human tissue plasminogen activator and urokinase genes.
B Rajput, S. Degen, E Reich, E. Waller, J Axelrod, R. Eddy, and T. Shows (1985)
Science 230, 672-674
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Evolution of proteolytic enzymes.
H Neurath (1984)
Science 224, 350-357
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Splice junctions: association with variation in protein structure.
C. Craik, W. Rutter, and R Fletterick (1983)
Science 220, 1125-1129
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Homology as Applied to Proteins.
W. P. Winter, K. A. Walsh, and H. Neurath (1968)
Science 162, 1433
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Aldolase and Protease: Unsuspected Structural Homology.
D. E. Morse and B. L. Horecker (1968)
Science 161, 813
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Amino Acid Sequences in Proteins.
P. H. Abelson (1968)
Science 160, 951
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Science. ISSN 0036-8075 (print), 1095-9203 (online)