Purification and characterization of a thermostable thiol protease from a newly isolated hyperthermophilic Pyrococcus sp

@article{Morikawa1994PurificationAC,
  title={Purification and characterization of a thermostable thiol protease from a newly isolated hyperthermophilic Pyrococcus sp},
  author={Masaaki Morikawa and Yoshihiro Izawa and Naeem Rashid and Toshihiro Hoaki and Tadayuki Imanaka},
  journal={Applied and Environmental Microbiology},
  year={1994},
  volume={60},
  pages={4559 - 4566}
}
A hyperthermophilic archaeon strain, KOD1, was isolated from a solfatara at a wharf on Kodakara Island, Kagoshima, Japan. The growth temperature of the strain ranged from 65 to 100 degrees C, and the optimal temperature was 95 degrees C. The anaerobic strain was an S0-dependent heterotroph. Cells were irregular cocci and were highly motile with several polar flagella. The membrane lipid was of the ether type, and the GC content of the DNA was estimated to be 38 mol%. The 16S rRNA sequence was… 

Purification and characterization of an intracellular heat-stable proteinase (pernilase) from the marine hyperthermophilic archaeon Aeropyrum pernix K1

Pernilase showed high substrate specificity for Boc-Leu-Gly-Arg-MCA peptide and Thermostability of this enzyme showed half-lives of 85 min at 100°C and 12 min at 110°C, suggesting that it corresponds to a serine proteinase.

Purification and Characterization of Two Functional Forms of Intracellular Protease PfpI from the Hyperthermophilic Archaeon Pyrococcus furiosus

PpI-C1 appears to be a predominant serine-type protease in cell extracts but is converted in vitro, probably in part by deamidation of Asn and Gln residues, to a more thermally stable form (PfpI-H) by prolonged heat treatment, and the deamination hypothesis is supported.

Cloning, Expression, and Characterization of Aminopeptidase P from the Hyperthermophilic Archaeon Thermococcus sp. Strain NA1

This study represents the first characterization of a hyperthermophilic archaeon APP, designated TNA1_APP (Thermococcus sp. strain NA1 APP), which was cloned and expressed in Escherichia coli and shown to be thermostable, with a half-life of >100 min at 80°C.

Characterization of recombinant glutamine synthetase from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1

The glnA gene encoding glutamine synthetase was cloned from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1, and its nucleotide sequence was determined. The glnA gene was expressed in

Gene Cloning and Characterization of Recombinant RNase HII from a Hyperthermophilic Archaeon

Results suggest that RNase HIIPk and E. coli RNases HI and HII are structurally and functionally related to one another.

A novel subtilisin-like serine protease from Thermoanaerobacter yonseiensis KB-1: its cloning, expression, and biochemical properties

Amo acid sequence comparison and phylogenetic analysis indicated that this enzyme belongs to a new subgroup with respect to its molecular evolution, when compared with previously characterized subtilisins.
...

References

SHOWING 1-10 OF 30 REFERENCES

An extremely thermostable extracellular proteinase from a strain of the archaebacterium Desulfurococcus growing at 88 degrees C.

An organism growing at 88 degrees C that closely resembles Desulfurococcus mucosus produced a single extracellular proteinase, which had an isoelectric point of 8.7, and was inhibited by di-isopropyl phosphorofluoridate, phenylmethanesulphonyl fluoride and chymostatin.

Characterization of sodium dodecyl sulfate-resistant proteolytic activity in the hyperthermophilic archaebacterium Pyrococcus furiosus

Cell extracts from Pyrococcus furiosus were found to contain five proteases, one of which (S66) are resistant to sodium dodecyl sulfate (SDS) denaturation, and results indicate that S66 is a serine protease.

Molecular cloning of a thermostable neutral protease gene from Bacillus stearothermophilus in a vector plasmid and its expression in Bacillus stearothermophilus and Bacillus subtilis

The structural gene for a thermostable protease from Bacillus stearothermophilus was cloned in plasmid pTB90 and it was found that the protease retained about 80% of its activity even after treatment of 65 degrees C for 30 min.

Regulation of Proteolytic Activity in the Hyperthermophile Pyrococcus furiosus

Under peptide-limiting conditions, levels of the 66-kDa protease (S66) were enhanced relative to those of other cell proteins, and preliminary evidence suggests that this protease is immunologically related to the eukaryotic multicatalytic proteinase complex (proteosome).

Deoxyribonucleic acid polymerase from the extreme thermophile Thermus aquaticus

A stable deoxyribonucleic acid (DNA) polymerase with a temperature optimum of 80 degrees C has been purified from the extreme thermophile Thermus aquaticus and is distinguished from the DNA polymerase of Escherichia coli.

Comparison of Extracellular Cellulase Activities of Clostridium thermocellum LQRI and Trichoderma reesei QM9414

  • T. NgJ. Zeikus
  • Biology, Chemistry
    Applied and environmental microbiology
  • 1981
The crude extracellular cellulase of Clostridium thermocellum LQRI (virgin strain) was very active and solubilized microcrystalline cellulose at one-half the rate observed for the extracellular

Enzymic properties of thermopsin.