Family U32
Summary for family U32
Family type peptidase | U32.001 - collagenase (Porphyromonas-type) (Porphyromonas gingivalis), MEROPS Accession MER0003242 (peptidase unit: 28-330) |
Content of family | Peptidase family U32 contains endopeptidases from bacteria. |
History |
Identifier created: Proteolysis in Cell Function, pp13-21, IOS Press, Amsterdam (1997) Proteolytic activity, usually described as 'collagenase', has been attributed to the product of the prtC gene of Porphyromonas gingivalis. |
Catalytic type | Peptidase of unknown catalytic type |
Active site | Nothing is known about the active site, and accordingly the peptidase is assigned to a family of unknown catalytic type. |
Activities and specificities | The PrtC peptidase (U32.001) was reported to degrade soluble and reconstituted fibrillar type I collagen, heat-denatured type I collagen, and azocoll, but not gelatin or a synthetic collagenase substrate (Kato et al., 1992). Activity of the homologue from Helicobacter pylori (U32.002) has been reported, but not characterised in detail (Kavermann et al., R., 2003). |
Inhibitors | The PrtC peptidase was inhibited by EDTA and thiol-blocking agents (Kato et al., 1992). |
Molecular structure | The PrtC peptidase ran as a band of 35 kDa in SDS gel electrophoresis, and the native enzyme behaved as a dimer in gel filtration chromatography (Kato et al., 1992). The deduced amino acid sequence shows no relationship to those of peptidases in any other family. |
Clan | unassigned |
Basis of clan assignment | Protein fold and active site residues are not known for any members of this family. |
Peptidases and Homologues |
MEROPS ID |
Structure |
collagenase (Porphyromonas-type) | U32.001 | Yes |
collagenase (Helicobacter-type) | U32.002 | - |
collagenase (Salmonella-type) | U32.003 | - |
Mername-AA261 putative peptidase (Clostridium beijerinckii) and similar | U32.004 | - |
YhbV protein (Escherichia coli) | U32.A01 | - |
yrrN g.p. (Bacillus subtilis) | U32.A02 | - |
Family U32 unassigned peptidases | unassigned | Yes |