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CATH Superfamily 2.40.10.10

Trypsin-like serine 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:

"
Trypsin-like serine 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 10: Kallikrein related peptidase 11

There are 1 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
Stratum corneum chymotryptic enzyme. [EC: 3.4.21.117]
Cleavage of proteins with aromatic side chains in the P1 position.
  • This enzyme has wide substrate specificity, being able to degrade heat-denatured bovine casein and the alpha-chain of native human fibrinogen.
  • It cleaves the B chain of bovine insulin at 6-Leu-|-Cya-7 (cysteic acid), 16-Tyr-|-Leu-17, 25-Phe-|-Tyr-26 and 26-Tyr-|-Thr-27.
  • It is thought to play a role in the desquamation (skin-shedding) of the outer layer of skin, the stratum corneum, by degrading intercellular cohesive structures.
  • Belongs to peptidase family S1A.
 8 A0A024R4H6 A0A024R4H6 A0A0B6VPC4 A0A0B6VPC4 P49862 P49862 Q91VE3 Q91VE3