Amino acid sequence of Streptomyces griseus protease B, a major component of pronase
Review articleOpen access

SummaryStreptomyces 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.

Request full text

References (0)

Cited By (0)

No reference data.
No citation data.
Join Copernicus Academic and get access to over 12 million papers authored by 7+ million academics.
Join for free!