Role of Intermolecular Disulfide Bonds of the Organic Solvent-Stable PST-01 Protease in Its Organic Solvent Stability
AUTOR(ES)
Ogino, Hiroyasu
FONTE
American Society for Microbiology
RESUMO
The PST-01 protease is secreted by the organic solvent-tolerant microorganism Pseudomonas aeruginosa PST-01 and is stable in the presence of various organic solvents. Therefore, the PST-01 strain and the PST-01 protease are very useful for fermentation and reactions in the presence of organic solvents, respectively. The organic solvent-stable PST-01 protease has two disulfide bonds (between Cys-30 and Cys-58 and between Cys-270 and Cys-297) in its molecule. Mutant PST-01 proteases in which one or both of the disulfide bonds were deleted were constructed by site-directed mutagenesis, and the effect of the disulfide bonds on the activity and the various stabilities was investigated. The disulfide bond between Cys-270 and Cys-297 in the PST-01 protease was found to be essential for its activity. The disulfide bond between Cys-30 and Cys-58 played an important role in the organic solvent stability of the PST-01 protease.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=92670Documentos Relacionados
- A role for intermolecular disulfide bonds in prion diseases?
- Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid-attachment site.
- Organic-Solvent-Tolerant Bacterium Which Secretes Organic-Solvent-Stable Lipolytic Enzyme
- Disulfide bonds and thermal stability in T4 lysozyme.
- Enhanced production and organic solvent stability of a protease fromBrevibacillus laterosporus strain PAP04
