|Family type peptidase||I88.001 - oryctin (Oryctes rhinoceros) (Oryctes rhinoceros), MEROPS Accession MER0202144 (inhibitor unit: 20-66)|
|Content of family||Family I88 contains serine endopeptidase inhibitors|
Identifier created: MEROPS 9.3 (7 September 2010)|
Oryctin (I88.001) was isolated from the hemolymph of the rhinoceros beetle (Oryctes rhinoceros). It was shown to be an inhibitor of bacterial and mammalian serine endopeptidases from families S1 and S8, but its physiological role in unknown (Horita et al., 2010).
|Peptidases inhibited||Peptidases inhibited include chymotrypsin A (S01.001), peptidase K (S08.054), subtilisin Carlsberg (S08.001) and elastase-2 (S01.131) (Horita et al., 2010).|
|Mechanism of inhibition||Oryctin is proposed to inhibit serine peptidases by the Laskowski mechanism also termed the 'standard' mechanism (Laskowski & Kato, 1980).|
|Molecular structure||The tertiary structure has been determined and the fold shown to be similar to that of Kazal inhibitors (family I1) but with the C-terminal strand replaced by a helix (Horita et al., 2010). Consequently, family I88 is included in clan IA.|