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CATH Superfamily 2.40.70.10

Acid Proteases

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Acid Proteases
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 24: Endothiapepsin

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Aspergillopepsin I. [EC: 3.4.23.18]
Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.
  • Found in a variety of Aspergillus species (imperfect fungi): A.awamori, A.foetidus, A.fumigatus, A.kawachii, A.niger, A.oryzae, A.saitoi, and A.sojae.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.23.6.
 64 A0A0J5Q5Z0 A0A0J5Q5Z0 A0A0J5Q5Z0 A0A0J5Q5Z0 A0A100IK58 A0A100IK58 A0A1S9D891 A0A1S9D891 A0A1S9D891 A0A1S9D891
(54 more...)
Penicillopepsin. [EC: 3.4.23.20]
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.
  • From the imperfect fungus Penicillium janthinellum.
  • Closely related enzymes have been isolated from P.roqueforti and P.duponti.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.17, EC 3.4.23.6 and EC 3.4.23.7.
 2 P78735 Q01972