NDLI: Regulation of Proteolytic Activity in the Hyperthermophile Pyrococcus furiosus

Content Provider	PubMed Central
Author	Snowden, Lesley J. Blumentals, Ilse I. Kelly, Robert M.
Abstract	Pyrococcus furiosus was shown to grow on casein or peptides as the sole carbon, energy, and nitrogen sources, while maltose could be used as a carbon and energy source only if peptides were present in the medium. A mixture of all 20 single amino acids could not replace the peptide requirement. Specific intracellular proteolytic activity was induced under low casein or tryptone levels and was decreased by the addition of maltose to both peptide-limiting and peptide-rich media in batch and continuous cultures. In a peptide-limited chemostat, activity towards azocasein and MeO-Suc-Arg-Pro-Tyr-p-nitroanilide reached a maximum at a dilution rate of 0.28 h-1, while activity toward l-lysine-p-nitroanilide reached a maximum at 0.50 h-1. Under peptide-limiting conditions, levels of the 66-kDa protease (S66) were enhanced relative to those of other cell proteins. Preliminary evidence suggests that this protease is immunologically related to the eukaryotic multicatalytic proteinase complex (proteosome).
Starting Page	1134
File Format	PDF
ISSN	10985336
e-ISSN	10985336
Journal	Applied and Environmental Microbiology
Issue Number	4
Volume Number	58
Language	English
Publisher Date	1992-04-01
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Ecology Food Science Applied Microbiology and Biotechnology Biotechnology

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Regulation of Proteolytic Activity in the Hyperthermophile Pyrococcus furiosus