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

L. Jurášek*, M. R. Carpenter, L. B. Smillie, A. Gertler, S. Levy, L. H. Ericsson

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

42 Scopus citations

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 languageEnglish
Pages (from-to)1095-1100
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume61
Issue number4
DOIs
StatePublished - 23 Dec 1974

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