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CATH Superfamily 3.40.630.10

Zn peptidases

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Zn peptidases
".

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 34806: probable leucine aminopeptidase 2

There are 7 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
Bacterial leucyl aminopeptidase. [EC: 3.4.11.10]
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
  • Similar aminopeptidases were isolated from Escherichia coli and Staphylococcus thermophilus.
  • Belongs to peptidase families M17 and M28.
 120 A0A069B7A0 A0A076W6T1 A0A080UNN6 A0A085F609 A0A085T813 A0A090IM73 A0A098G0R2 A0A098GAQ6 A0A099KNH9 A0A099KSM9
(110 more...)
Aminopeptidase Y. [EC: 3.4.11.15]
Preferentially, release of N-terminal lysine.
  • Inhibited by Zn(2+) and Mn(2+).
  • Hydrolyzes L-lysyl-4-nitroanilide and, more slowly, L-arginyl-4- nitroanilide.
  • Belongs to peptidase family M28B.
 95 A0A0A1FK05 A0A0A1FPK3 A0A0A8X646 A0A0B9A713 A0A0D6GMY4 A0A0D6T686 A0A0D6ULE2 A0A0D6UYA5 A0A0F6J7I0 A0A0G8C3G1
(85 more...)
Aminopeptidase S. [EC: 3.4.11.24]
Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues.
  • Activated by Ca(2+).
  • In the presence of Ca(2+), the best substrates are Leu-Phe, Leu-Ser, Leu-pNA (aminoacyl-p-nitroanilide), Phe-Phe-Phe and Phe-Phe.
  • Peptides with proline in the P1' position are not substrates.
  • Belongs to peptidase family M28.
  • Formerly EC 3.4.11.n1.
 64 A0A0M2HC11 A0A0M2HMQ0 A0A0N1FZU8 A0A0N1GFS5 A0A0N1GZ84 A0A0N1NTU1 A0A0T8L6W5 A0A0T9KML8 A0A0T9M382 A0A0U0WR69
(54 more...)
Aminopeptidase B. [EC: 3.4.11.6]
Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.
  • Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds.
  • One of the activities of the bifunctional enzyme EC 3.3.2.6.
  • Belongs to peptidase family M1.
 40 A0A0D1RGU8 A0A0E8T9K8 A0A0F6J7I0 A0A0H4RSP6 A0A0J7CD28 A0A0K6J823 A0A0K6JRI5 A0A0K6KJF1 A0A0K6LA18 A0A0K6LQ62
(30 more...)
Leucyl aminopeptidase. [EC: 3.4.11.1]
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
  • Is activated by heavy metal ions.
  • Belongs to peptidase family M17.
  • Formerly EC 3.4.1.1.
 31 A0A045J2P3 A0A0E1AWC8 A0A0H3L9G7 A0A0H3M264 A0A0H3P4A3 A0A0H3Q5M6 A0A0H5T5B1 A0A0K2HSV9 A0A0K9UYR3 A0A0P1DAJ0
(21 more...)
Vibriolysin. [EC: 3.4.24.25]
Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favored residue, which distinguished this enzyme from thermolysin.
  • Thermostable enzyme from Vibrio proteolyticus (formerly Aeromonas proteolytica).
  • Specificity related to, but distinct from, those of the thermolysin and Bacillus subtilis endopeptidase.
  • Belongs to peptidase family M4.
  • Formerly EC 3.4.24.4.
 3 A0A099KSM9 A0A099LI88 A0A0M8KJG6
Glutamate carboxypeptidase II. [EC: 3.4.17.21]
Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.
  • Hydrolyzes alpha-peptide bonds in Ac-Asp-Glu, Asp-Glu, and Glu-Glu, but also gamma-glutamyl bonds in gamma-Glu-Glu and folylpoly-gamma- glutamates.
  • With folylpoly-gamma-glutamates, shows processive carboxypeptidase activity to produce pteroylmonoglutamate.
  • Does not hydrolyze Ac-beta-Asp-Glu.
  • Inhibited by quisqualic acid, Ac-beta-Asp-Glu, and 2-phosphonomethyl- pentanedioate.
  • The release of C-terminal glutamate from folylpoly-gamma-glutamates is also catalyzed by EC 3.4.17.11 and EC 3.4.19.9.
  • Belongs to peptidase family M28.
  • Formerly EC 3.4.19.8.
 2 A4F682 Q0SEP4
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