Thermopsin is a peptidase from Sulfolobus acidocaldarius that is active at low pH and high temperature. From reversible inhibition with pepstatin, thermopsin is thought to be an aspartic peptidase. It is a member of the only family of peptidases to be restricted entirely to the archaea, namely peptidase family A5. Evolution within this family has been mapped, using a taxonomic tree based on the known classification of archaea. Homologues are found only in archaeans that are both hyperthermophiles and acidophiles, and this implies lateral transfer of genes between archaea, because species with homologues are not necessarily closely related. Despite the remarkable stability and activity in extreme conditions, no tertiary structure has been solved for any member of the family, and the catalytic mechanism is unknown. Putative catalytic residues have been predicted here by examination of aligned sequences.
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From volcanoes to the bench: Advantages of novel hyperthermoacidic archaeal proteases for proteomics workflows.
J Proteomics
October 2023
Department of Biochemistry and Molecular Genetics, University of Colorado Denver, Aurora, CO 80045, USA. Electronic address:
Here we introduce hyperthermoacidic archaeal proteases (HTA-Proteases©) isolated from organisms that thrive in nearly boiling acidic volcanic springs and investigate their use for bottom-up proteomic experiments. We find that HTA-Proteases have novel cleavage specificities, show no autolysis, function in dilute formic acid, and store at ambient temperature for years. HTA-Proteases function optimally at 70-90 °C and pH of 2-4 with rapid digestion kinetics.
View Article and Find Full Text PDFA new pepstatin-insensitive thermopsin-like protease overproduced in peptide-rich cultures of Sulfolobus solfataricus.
Int J Mol Sci
February 2014
Institute of Biosciences and BioResources, National Research Council (CNR-IBBR), Via Pietro Castellino 111, Naples 80131, Italy.
In this study, we gain insight into the extracellular proteolytic system of Sulfolobus solfataricus grown on proteinaceous substrates, providing further evidence that acidic proteases were specifically produced in response to peptide-rich media. The main proteolytic component was the previously isolated SsMTP (Sulfolobus solfataricus multi-domain thermopsin-like protease), while the less abundant (named SsMTP-1) one was purified, characterized and identified as the sso1175 gene-product. The protein revealed a multi-domain organization shared with the cognate SsMTP with a catalytic domain followed by several tandemly-repeated motifs.
View Article and Find Full Text PDFEvolution of the thermopsin peptidase family (A5).
PLoS One
September 2014
Wellcome Trust Sanger Institute, Hinxton, Cambridgeshire, United Kingdom ; European Molecular Biology Laboratory, European Bioinformatics Institute, Hinxton, Cambridgeshire, United Kingdom.
Thermopsin is a peptidase from Sulfolobus acidocaldarius that is active at low pH and high temperature. From reversible inhibition with pepstatin, thermopsin is thought to be an aspartic peptidase. It is a member of the only family of peptidases to be restricted entirely to the archaea, namely peptidase family A5.
View Article and Find Full Text PDFIdentification of a cell-bound extracellular protease overproduced by Sulfolobus solfataricus in peptide-rich media.
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January 2010
IBP-Consiglio Nazionale delle Ricerche, Via Pietro Castellino 111, 80131 Napoli, Italy.
A new protease, named SsMTP was identified from the archeon Sulfolobus solfataricus. The enzyme is associated to the cell-membrane and over-produced in response to the peptide-enriched media. SsMTP has a molecular mass of 120 kDa showing optimal activity at pH 2.
View Article and Find Full Text PDFThermopsin.
Methods Enzymol
October 1995
Protein Studies Program, Oklahoma Medical Research Foundation, Oklahoma City 73104, USA.
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