Amino acid sequence of endothiapepsin. Complete primary structure of the aspartic protease from Endothia parasitica.
The amino acid sequence of endothiapepsin, the aspartic protease from Endothia parasitica has been determined. The enzyme consists of 330 residues. The sequence determination was performed exclusively at the protein level. The homology of this fungal milk-clotting enzyme with aspartic proteases is demonstrated by alignment with pepsin, chymosin, gastricsin, renin, and cathepsin D from various vertebrates and proteinase A from Saccharomyces cerevisiae showing 25-30% identity. The identity with mucor rennin from Mucor pucillus was 21% and with penicillopepsin from Penicillium janthinellum 53%, the fungal enzymes thus representing the lowest as well as the highest degree of homology.
Barkholt
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D000595:Amino Acid Sequence; D000818:Animals; D001203:Ascomycota / Q000201:enzymology*; D016282:Aspartic Acid Endopeptidases; D010450:Endopeptidases / Q000032:analysis* / Q000235:genetics; D006801:Humans; D010449:Peptide Mapping
D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; C042466:Endothia aspartic proteinase