Abstract
Streptomyces griseus Protease B is a close homologue of Protease A, another serine protease isolated from Pronase. Homology based on identity of residues in the two enzymes is 61%. Extensive identical sequences are found in the vicinities of histidine-57, aspartic acid-102, serine-195, the two disulfide bridges, the NH2-terminal and COOH-terminal ends as well as in the region of the presumed substrate binding sites. However, certain regions of the Protease B sequence are markedly different and include a heptapeptide insertion between residues 88 and 89 and a tetrapeptide deletion between residues 129 and 136 when compared with Protease A. These differences are probably responsible for the remarkable stability of Protease B in concentrated solutions of urea and guanidine hydrochloride.
| Original language | English |
|---|---|
| Pages (from-to) | 1095-1100 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 61 |
| Issue number | 4 |
| DOIs | |
| State | Published - 23 Dec 1974 |
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