Thermopsin
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.23 Aspartic endopeptidases > 3.4.23.42 thermopsin
Thermopsin is an aspartic endopeptidase from the thermophilic archaeon Sulfolobus acidocaldarius, maximally active at pH 2 and 90 °C, weakly inhibited by pepstatin but with no sequence similarity to pepsin; it is the type example of peptidase family A5 and occurs in Archaea and Eukaryota. Its specificity resembles pepsin A, preferring bulky hydrophobic amino acids at P1 and P1'. In the acidothermophile it digests proteins under extreme hot-acid conditions. It features a thermostable aspartic-protease fold unrelated to pepsin.
Thermopsin is an aspartic endopeptidase from the thermophilic archaeon Sulfolobus acidocaldarius, maximally active at pH 2 and 90 °C, weakly inhibited by pepstatin but with no sequence similarity to pepsin; it is the type example of peptidase family A5 and occurs in Archaea and Eukaryota. Its specificity resembles pepsin A, preferring bulky hydrophobic amino acids at P1 and P1'. In the acidothermophile it digests proteins under extreme hot-acid conditions. It features a thermostable aspartic-protease fold unrelated to pepsin.
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