| Autor: |
Venot, Nicole, Sciaky, Martine, Puigserver, Antoine, Desnuelle, Pierre, Laurent, Georgette |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 5/15/86, Vol. 157 Issue 1, p91-99, 9p |
| Abstrakt: |
The sequence of the 240 amino acids and the position of the five S-S bridges of subunit III of the bovine pancreatic 6 S procarboxypeptidase A complex have been determined thus confirming its phylogenetic filiation with the pancreatic serine endopeptidase group. The subunit contains at equivalent positions ali the elements of the catalytic site of these enzymes. The elements or a binding pocket very similar to that of porcine elastase I are also present in the protein thus accounting for its zymogen-like activity. The most obvious difference is the absence in the subunit of the two strongly hydrophobic amino acids (16 and 17 in the chymotrypsinogen numbering), which are known to participate in the stabilization of a fully functional binding pocket inactive endopeptidases. Four of the five disulfide bridges of subunit III are homologous with those common to all pancreatic endopeptidases. In contrast the fifth bridge forms a very small loop of only four amino acids, which is not encountered in active endopeptidases. Other potentially lethal modifications in the structure of the subunit are not excluded. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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