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Atlantic cod cDNA encoding a psychrophilic chymotrypsinogen

A Guthmundsdóttir¹, S Oskarsson, A E Eakin

¹Science Institute, University of Iceland, Reykjavík.

Biochimica Et Biophysica Acta

|September 13, 1994

Summary

Researchers isolated and characterized a psychrophilic cod chymotrypsinogen cDNA clone. This study reveals unique features in the cod enzyme

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Area of Science:

Biochemistry
Molecular Biology
Enzymology

Background:

Chymotrypsinogens are key digestive enzymes.
Understanding enzyme adaptations in psychrophilic organisms is crucial.

Purpose of the Study:

To isolate and characterize the cDNA encoding chymotrypsinogen from a psychrophilic cod.
To analyze the structural and sequence features of this cold-adapted enzyme.

Main Methods:

cDNA cloning and sequencing.
Bioinformatic analysis of the predicted amino acid sequence.

Main Results:

A cDNA clone for psychrophilic cod chymotrypsinogen was successfully isolated.
The predicted preproenzyme consists of 263 amino acids, including an 18-residue signal sequence.

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Cod chymotrypsinogen shares 64-68% amino acid identity with mammalian counterparts, with notable proline residue substitutions.

Conclusions:

The isolated cod chymotrypsinogen exhibits unique sequence characteristics potentially related to its psychrophilic adaptation.
Comparative analysis highlights conserved and divergent features between cold-adapted and mammalian chymotrypsinogens.