Proteinase structure-function relationships

Mierzwa, S., and Chan, S. K. (1987). Chemical modification of human alpha 1 proteinase inhibitor by tertanitromethane. Structure-function relationship. Biochem.J. 246,37-42. 

Pepsin (EC 3.4.23.1) is a typical aspartic proteinase produced in the gastric mucosa of vertebrates as a zymogen form [10], This enzyme has been extensively characterized, and its three-dimensional structure has been determined at high resolution. Porcine pepsin, in particular, has been studied as model to analyze the structure-function relationship of the aspartic proteinases. Although the aspartic proteinases including mammalian and fungal enzymes are quite similar in their three-dimentional structures, there are drastic differences in the catalytic properties, especially in substrate specificities. 

Huber, R., and Bennett, W. S., Jr. (1982). Functional significance jof flexibility In proteins. Pure Appl. Chem. 54, 2489-2500. Ikenaka, T., and Odani, S. (1978). Structure-function relationships of soybean double-headed proteinase Inhibitors. In "Regulatory Proteolytic Enzymes and Their Inhibitors." TProc. 11th FEBS Meeting), S. Magnusson, M. Ottesen, B. Foltmann,... 

The alignment in Table I includes sequences from 12 different zymogens and enzymes, only two of which are known completely and a third is almost completed. Despite the fragmentary data, we are able to deduct some general structure-function relationships of the aspartate proteinases and of the gastric zymogens. 

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