Family I36
Summary for family I36
| Name | Inhibitor family I36 (SMI family) |
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| Family type peptidase | I36.001 - Streptomyces metallopeptidase inhibitor (Streptomyces nigrescens), MEROPS Accession MER0018465 (inhibitor unit: 30-131) |
| Content of family | Inhibitor family I36 contains an inhibitor of metalloendopeptidases. |
| History |
Identifier created: MEROPS 6.1 (10 January 2003)
The Streptomyces metallopeptidase inhibitor (I36.001) was discovered by Oda et al. (1979). |
| Peptidases inhibited | Peptidases inhibited are in family M4 (Hiraga et al., 1999). Thermolysin (M04.001) was the first peptidase to be found to be inhibited (Oda et al., 1979), but pseudolysin (M04.005) and griselysin (as Streptomyces griseus metalloproteinase II: M04.017) are inhibited still more potently (Seeram et al., 1997). |
| Mechanism of inhibition | Streptomyces metallopeptidase inhibitor has been reported to interact with metallopeptidases by the Laskowski mechanism (Seeram et al., 1997; Hiraga et al., 1999) that is normally seen with inhibitors of serine peptidases. The reactive site loop is less flexible than those of many serine peptidase inhibitors (Tate et al., 1998). The way in which the components of the enzyme-inhibitor complex interact has been predicted on the basis of their uncomplexed structures (Tate et al., 1998). |
| Molecular structure | The protein of 102 amino acid residues contains two small disulfide loops (seven and six residues, respectively: Murai et al., 1985). The reactive site bond is in the second of these (Seeram et al., 1997). A high-resolution solution structure shows that the molecule is composed of two beta-sheets, each consisting of four antiparallel beta-strands (Ohno et al., 1998). |
| Clan | IU |
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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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| Inhibitors and Homologues |
MEROPS ID |
Structure |
| Streptomyces metallopeptidase inhibitor | I36.001 | Yes |
| Family I36 unassigned peptidases | unassigned | - |
