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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 32: Kallikrein 1-related peptidase C9

There are 4 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
Tissue kallikrein. [EC: 3.4.21.35]
Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.
  • Formed from tissue prokallikrein by activation with trypsin.
  • A large number of tissue kallikrein-related sequences have been reported for rats and mice, though fewer seem to exist in other mammals.
  • The few that have been isolated and tested on substrates include mouse EC 3.4.21.54, submandibular proteinase a, epidermal growth- factor-binding protein, nerve growth factor gamma-subunit, rat tonin, submaxillary proteinases A and B, T-kininogenase, kallikreins K7 and K8.
  • The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-|-Xaa bonds.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.21.8.
 57 A0A024R4J4 A0A024R4J4 A0A0B6VSQ6 A0A0B6VSQ6 A0A1R3UCD2 A0A1R3UCD2 A0A1R3UCH6 A0A1R3UCH6 A0A1R3UCJ3 A0A1R3UCJ3
(47 more...)
Semenogelase. [EC: 3.4.21.77]
Preferential cleavage: -Tyr-|-Xaa-.
  • Slowly inhibited by alpha-1-antichymotrypsin.
  • Belongs to peptidase family S1.
 9 G7NMC9 G7NMC9 P07288 P07288 P33619 P33619 Q546G3 Q546G3 Q6DT45
Gamma-renin. [EC: 3.4.21.54]
Cleavage of the Leu-|-Leu bond in synthetic tetradecapeptide renin substrate, to produce angiotensin I, but not active on natural angiotensinogen. Also hydrolyzes Bz-Arg-p-nitroanilide.
  • Unlike EC 3.4.23.15, does not act on natural angiotensinogen.
  • A member of the tissue kallikrein family, from submandibular glands of male mice.
  • Belongs to peptidase family S1.
 4 A0A1R3UCH4 A0A1R3UCH4 P04071 P04071
Kallikrein 13. [EC: 3.4.21.119]
Hydrolyzes mouse Ren2 protein (a species of prorenin present in the submandibular gland) on the carboxy side of the arginine residue at the Lys-Arg-|- pair in the N-terminus, to yield mature renin.
  • Specific for prorenin from the mouse submandibular gland, as prorenin from the mouse kidney (Ren1) and human prorenin are not substrates.
  • Site-directed mutagenesis studies have shown that the enzyme will also cleave prorenin when Lys-Arg is replaced by Arg-Arg or Gln-Arg but the rate of reaction is much slower when Lys-Lys is used.
  • Also able to process pro-interleukin-1-beta (pro-IL-1-beta) in mouse submandibular gland to form IL-1-beta.
  • Belongs to peptidase family S1A.
 1 P36368
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