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 17: Chymotrypsin-like elastase family member 1

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
Pancreatic elastase. [EC: 3.4.21.36]
Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.
  • Formed by activation of proelastase from mammalian pancreas by trypsin.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.7 and EC 3.4.21.11.
11 A0A480DJK8 A0A480DJK8 O46644 P00772 P00772 P00773 Q28153 Q5R1M5 Q867B0 Q91X79
(1 more...)
Pancreatic elastase II. [EC: 3.4.21.71]
Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.
  • Formed by activation of proelastase II from mammalian pancreas by trypsin.
  • Usually, only one of the pancreatic elastases (see also EC 3.4.21.36) is expressed in a given species; human pancreatic elastase is of type II.
  • Belongs to peptidase family S1.
6 P00774 P05208 P08217 P08218 P08419 Q29461
Pancreatic endopeptidase E. [EC: 3.4.21.70]
Preferential cleavage: Ala-|-Xaa. Does not hydrolyze elastin.
  • From pancreatic juice.
  • Unlike elastases, has an acidic pI.
  • Binds cholesterol.
  • Belongs to peptidase family S1.
4 O19023 P08861 P09093 Q9CQ52
Chymotrypsin C. [EC: 3.4.21.2]
Preferential cleavage: Leu-|-Xaa, Tyr-|-Xaa, Phe-|-Xaa, Met-|-Xaa, Trp-|-Xaa, Gln-|-Xaa, Asn-|-Xaa.
  • Reacts more readily with Tos-Leu-CH(2)Cl than Tos-Phe-CH(2)Cl, in contrast to chymotrypsin.
  • Belongs to peptidase family S1.
3 P55091 Q3SYP2 Q99895