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CATH Superfamily 3.30.830.10

Metalloenzyme, LuxS/M16 peptidase-like

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:

"
Metalloenzyme, LuxS/M16 peptidase-like
".

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 12: Protease 3

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
Pitrilysin. [EC: 3.4.24.55]
Preferential cleavage of 16-Tyr-|-Leu-17 and 25-Phe-|-Tyr-26 bonds of oxidized insulin B chain. Also acts on other substrates of Mw less than 7 kDa such as insulin and glucagon.
  • From the periplasmic space of Escherichia coli.
  • Inhibited by EDTA and 1,10-phenanthroline; not thiol dependent.
  • Belongs to peptidase family M16.
  • Formerly EC 3.4.99.44.
 450 A0A024LA55 A0A024LA55 A0A024LA55 A0A024LA55 A0A024LA55 A0A024LA55 A0A024LA55 A0A024LA55 A0A024LA55 A0A024LA55
(440 more...)
Nardilysin. [EC: 3.4.24.61]
Hydrolysis of polypeptides, preferably at -Xaa-|-Arg-Lys-, and less commonly at -Arg-|-Arg-Xaa-, in which Xaa is not Arg or Lys.
  • Unusually for a metallopeptidase, inhibited by bestatin, amastin and ethylmaleimide.
  • Belongs to peptidase family M16.
 4 A0A178WD59 A0A178WD59 F4HNU6 F4HNU6