Abstract
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 2.0 in the temperature range 70 - 90 degrees C, and a half-life of 20 days at 80 degrees C. Primary structure analysis revealed that SsMTP represents a novel type of multi-domain thermopsin-like protease containing the catalytic domain followed by two distinct domains, PKD and Y_Y_Y, which are usually involved in a range of protein-protein interactions among the extracellular proteins.
MeSH terms
-
Amino Acid Sequence
-
Bacterial Proteins
-
Culture Media
-
Electrophoresis, Polyacrylamide Gel
-
Endopeptidases / chemistry
-
Gelatin / chemistry
-
Gelatin / metabolism
-
Mass Spectrometry
-
Membrane Proteins / biosynthesis*
-
Membrane Proteins / chemistry
-
Membrane Proteins / genetics
-
Membrane Proteins / metabolism
-
Molecular Sequence Data
-
Peptide Hydrolases / biosynthesis*
-
Peptide Hydrolases / chemistry
-
Peptides / metabolism
-
Protein Structure, Tertiary
-
Sequence Alignment
-
Sulfolobus solfataricus / enzymology*
-
Sulfolobus solfataricus / genetics
-
Sulfolobus solfataricus / metabolism
Substances
-
Bacterial Proteins
-
Culture Media
-
Membrane Proteins
-
Peptides
-
Gelatin
-
Endopeptidases
-
Peptide Hydrolases
-
thermopsin