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CATH Superfamily 1.10.390.10

Neutral Protease Domain 2

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:

"
Neutral Protease Domain 2
".

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 5149: Peptidase, M4 (Thermolysin) family

There are 8 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
Bacillolysin. [EC: 3.4.24.28]
Similar, but not identical, to that of thermolysin.
  • Variants of this enzyme have been found in species of Bacillus including B.subtilis, B.amyloliquefaciens, B.megaterium, B.mesentericus, B.cereus and B.stearothermophilus.
  • Belongs to peptidase family M4.
  • Formerly EC 3.4.24.4.
 401 A0A023P0D4 A0A023P7N8 A0A068NDY4 A0A068NE84 A0A075R1Q7 A0A076VXZ2 A0A076W2D8 A0A077MZ73 A0A077N2F7 A0A077NNV3
(391 more...)
Aureolysin. [EC: 3.4.24.29]
Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1' residues. Activates the glutamyl endopeptidase (EC 3.4.21.19) of Staphylococcus aureus.
  • Earlier confused with staphylokinase.
  • Belongs to peptidase family M4.
  • Formerly EC 3.4.24.4 and EC 3.4.99.22.
 94 A0A068E656 A0A077UVZ8 A0A0A8X0L7 A0A0A8X622 A0A0B5S5G9 A0A0D6T2B8 A0A0E0VTT6 A0A0E1AKF2 A0A0E1VMC1 A0A0E1XAY9
(84 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.
 85 A0A090RWN3 A0A090SDP2 A0A090T886 A0A098GAG9 A0A099KY68 A0A099LHS9 A0A0A1FF14 A0A0A3ES28 A0A0A8UNU9 A0A0A8UTE8
(75 more...)
Thermolysin. [EC: 3.4.24.27]
Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.
  • A thermostable extracellular metalloendopeptidase containing four calcium ions.
  • Enzymes that may be species variants of thermolysin are reported from Micrococcus caseolyticus and Aspergillus oryzae.
  • Closely related but distinct enzymes are aeromonolysin, pseudolysin, bacillolysin, aureolysin and mycolysin.
  • Belongs to peptidase family M4.
  • Formerly EC 3.4.24.4.
 74 A0A0D8BHM5 A0A0D8BQ54 A0A0E0TFP6 A0A0F6J1J3 A0A0G3Y3S3 A0A0K0Q2H9 A0A0K6J964 A0A0N0MML5 A0A0N0MMM1 A0A0N0NDA0
(64 more...)
Pseudolysin. [EC: 3.4.24.26]
Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects.
  • Causes tissue damage.
  • Belongs to peptidase family M4.
  • Formerly EC 3.4.24.4.
 37 A0A090RWN3 A0A090SDP2 A0A090T886 A0A099K8F1 A0A0C5VQV5 A0A0D6STS0 A0A0D8ZFL3 A0A0E1ATG1 A0A0E4GFE9 A0A0H3R469
(27 more...)
Endopeptidase La. [EC: 3.4.21.53]
Hydrolysis of proteins in presence of ATP.
  • ATP hydrolysis is linked with peptide bond hydrolysis.
  • Vanadate inhibits both reactions.
  • A similar enzyme occurs in animal mitochondria.
  • Belongs to peptidase family S16.
 1 A0A0K1EGV2
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase. [EC: 2.1.1.14]
5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine.
  • Requires phosphate.
  • The enzyme from Escherichia coli also requires a reducing system.
  • Unlike EC 2.1.1.13 this enzyme does not contain cobalamin.
 1 A8T9E8
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.
 1 A0A099KUB5