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Fig. 4. Multiple alignment of the deduced amino acid sequence of the serine
protease domain of S. haematocheir OHSS with those of known serine
proteases of six species. Regions of high homology across all species are
highlighted in black (100–90%); regions with less homology are
highlighted in gray (>80%) and purple (>60%). The numbering of amino
acids corresponds to the original sequences in each animal. Information for
comparison: chymotrypsin of Penaeus vanameii (database accession
number S29239); trypsin of Paralithodes camtschaticus (AF461036);
proclotting enzyme (procl.) of Tachypleus tridentatus (P21902);
defensin of Pacifastacus leniusculus (AJ007668.1); human hepsin
(P05981); human matriptase (Q9Y5Y6). Residues in the catalytic triad (His-293,
Asp-346 and Ser-441) are indicated by an asterisk. Residues in the substrate
pocket (Asp-435, Gly-463 and Gly-473) are indicated by diamonds. Six
conservative cysteines needed to form three intramolecular disulfide bonds are
likely pairings as follows: Cys278–Cys294, Cys411–Cys426, and
Cys437–Cys466. The disulfide bond Cys246–Cys366 (the cysteines are
boxed) is observed in two-chain serine proteases, but not in trypsin and
chymotrypsin.
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