Family S37
Summary for family S37
Family type peptidase | S37.001 - PS-10 peptidase (Streptomyces lividans), MEROPS Accession MER0001350 (peptidase unit: 27-474) |
Content of family | Family S37 contains a tripeptidyl-peptidase from Streptomyces. |
History |
Identifier created: Proteolysis in Cell Function, pp13-21, IOS Press, Amsterdam (1997)
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Catalytic type | Serine |
Active site residues | S168 D368 H399 |
Active site | Active site residues have not been determined for any member of this family, and the active site triad is hypothetical. As can be seen from the Alignment for clan SC, the pattern of conserved glycines around the proposed active site serine and histidine residues in family S37 is consistent with that of other families in this clan. |
Activities and specificities | The peptidase from Streptomyces mobaraensis has been shown to activate the transglutaminase precursor by removal of a leading tri- or tetrapeptide (Umezawa et al., 2004). Calcium ions enhance activity (Zotzel et al., 2003). |
Inhibitors | PS-10 peptidase (S37.001) is inhibited by the generic serine peptidase inhibitor PMSF (Umezawa et al., 2004). |
Molecular structure | No tertiary structure has been determined for any member of the family. Peptidases in family S37 are synthesized with signal peptides (Umezawa et al., 2004). |
Clan | SC |
Basis of clan assignment | Active site residues for members of this family and family S10 occur in the same order in the sequence: S, D, H. |
Distribution of family
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Bacteria |
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Archaea |
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Protozoa |
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Fungi |
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Plants |
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Animals |
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Viruses |
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