Title: THE PROTEOLYTIC ENZYMES OF THE K-1 STRAIN OF STREPTOMYCES GRISEUS OBTAINED FROM A COMMERCIAL PREPARATION (PRONASE). XI. EVOLUTIONARY IMPLICATIONS
Abstract: Abstract: Different Pronase proteolytic components show genetic relationships with either mammalian or microbial proteases. Three endopeptidases are homologous with pancreatic serine endopeptidases; they are a trypsin and two enzymes named chymoelastases because of activities resembling both chymotrypsin and elastase. These three endopeptidases have diverged in structure and function during phylogeny. Pronase trypsin, like the bovine homolog, cannot be acetylated at the single α-amino residue. In contrast each chymoelastase can be acetylated at the single amino terminus without significant change in activity. A fourth serine enzyme possesses properties which are very similar to those of the subtilisins. A carboxypeptidase has been purified and shows characteristics which strongly suggest homology with bovine pancreatic carboxypeptidase A. Like the bovine enzyme, Pronase carboxypeptidase is a zinc containing protein. These studies suggest that the association of the chymotrypsin enzyme family with pancratic carboxypeptidase was established very early during the course of evolution. Two Pronase aminopeptidases have been purified and studies reveal that they are probably products of single gene origin with limited proteolysis generating two microheterogeneous forms.
Publication Year: 1976
Publication Date: 1976-01-01
Language: en
Type: book-chapter
Indexed In: ['crossref']
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Cited By Count: 2
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