P. Hernandez-cortes et al., Trypsin from Pacifastacus leniusculus hepatopancreas: Purification and cDNA cloning of the synthesized zymogen, BIOL CHEM, 380(4), 1999, pp. 499-501
Trypsin was purified from crayfish, Pacifastacus leniusculus, hepatopancrea
s, and the gene that encoded this enzyme was cloned from a hepatopancreas c
DNA library. Crayfish trypsin is synthesized as a zymogen according to the
sequence of the putative precursor peptide. The authenticity of the trypsin
ogen is supported by the deduced amino acid sequence and confirmed by the N
-terminal amino acid sequence of the mature protein. The enzyme has feature
s characteristic of a trypsin, such as a specific binding pocket. Sequence
comparison shows that crayfish trypsin is similar to those of other species
, with the exception that six cysteine residues present in vertebrates are
missing. Some structural characteristics, such as the length of the signal
peptide and a calcium binding site, are similar to bacterial trypsin.