Active subtilisin-like protease from a hyperthermophilic archaeon in a form with a putative prosequence

Article Abstract:

The characteristics of a subtilisin-like protease from Thermococcus kodakaraensis KOD1 are described. Unlike other bacterial subtilisins, the folded enzyme includes a putative prosequence. It has broad substrate specificity, but prefers aromatic and large nonpolar P1 substrates.

Proteases, Microbial enzymes

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[Ca.sup.2+]-dependent maturation of subtilisin from a hyperthermophilic archaeon, Thermococcus kodakaraensis: The propeptide is a potent inhibitor of the mature domain but is not required for its folding

Article Abstract:

Thermococcus kodakaraensis mat-subtilitsin and T. kodakaraensis pro-subtilisin were subjected to SDS-PAGE, and their protease activities were analyzed by activity staining of the gel at 20 and 80 degree Celsius in order to confirm that T. kodakaraensis mat-subtilisin refolded in the absence of propeptide exhibits [Ca.sup.2+]- dependent activity. It is proved that both the proteins exhibited actively, at the positions to which they migrated, only in presence of [Ca.sup.2+]- and not in the absence of [Ca.sup.2+].

Science & research, Pharmaceutical Preparation Manufacturing, All Other Basic Inorganic Chemical Manufacturing, Pharmaceutical preparations, Industrial inorganic chemicals, not elsewhere classified, Calcium, Calcium Supplements, Bacterial genetics, Protein folding, Calcium (Nutrient), Bacterial proteins, Calcium, Dietary, Structure, Chemical properties

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Isolation and characterization of a second subunit of molecular chaperonin from Pyrococcus kodakaraensis KOD1: analysis of an ATPase-deficients mutant enzyme

Article Abstract:

A study was conducted to investigate the chaperonin functions of Pyrococcus kodakaraensis genes KOD1 CpkA and CpkB when they are coexpressed with cobyric acid synthase (CobQ) in Escherichia coli. Results indicate that both genes are capable of reducing the amount of insoluble form of CobQ. It was also observed that both CpkA and CpkB have the same adenosine triphosphatase activity like other bacterial and eukaryal chaperonins.

Usage, Physiological aspects, Gene expression, Genetic recombination, Adenosine triphosphatase

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