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Multiple functions of pro‐parts of aspartic proteinase zymogens
Author(s) -
Koelsch Gerald,
Mareš Michael,
Metcalf Peter,
Fusek Martin
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80596-2
Subject(s) - aspartic acid , structure function , biochemistry , chemistry , folding (dsp implementation) , function (biology) , biology , computational biology , microbiology and biotechnology , amino acid , engineering , physics , particle physics , electrical engineering
The importance of aspartic proteinases in human pathophysiology continues to initiate extensive research. With burgeoning information on their biological functions and structures, the traditional view of the role of activation peptides of aspartic proteinases solely as inhibitors of the active site is changing. These peptide segments, or pro‐parts, are deemed important for correct folding, targeting, and control of the activation of aspartic proteinase zymogens. Consequently, the primary structures of pro‐parts reflect these functions. We discuss guidelines for formation of hypotheses derived from comparing the physiological function of aspartic proteinases and sequences of their pro‐parts.