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Article

The prosequence of thermolysin acts as an intramolecular chaperone when expressed in trans with the mature sequence in Escherichia coli.

Journal of molecular biology - 5 Feb 1999

Marie-Claire C, Ruffet E, Beaumont A, Roques B P

Abstract excerpt

The zinc metalloendopeptidase, thermolysin (EC 3.4.24.27) produced by Bacillus thermoproteolyticus serves as a model of important physiological enzymes such as neprilysin, angiotensin converting enzyme and endothelin converting enzyme. Thermolysin is synthesised as a pre-proenzyme, with an N-terminal prosequence of 204 residues and a mature sequence of 316 residues. The prosequence facilitates the folding of the...

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Identifiers

PMID: 9925774
DOI: 10.1006/jmbi.1998.2449

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