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A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

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Published on: November 7, 2012

Thermostable aminopeptidase from Pyrococcus horikoshii.

S Ando¹, K Ishikawa, H Ishida

¹National Institute of Bioscience and Human-Technology, Tsukuba, Ibaraki, Japan.

|April 28, 1999

Summary

Researchers identified a novel thermostable aminopeptidase from Pyrococcus horikoshii. This enzyme efficiently removes N-terminal amino acids from peptides at high temperatures, aiding in peptide sequence analysis.

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Area of Science:

Biochemistry
Enzymology
Extremophile Biology

Background:

Genomic analysis of thermophilic archaea can reveal novel enzymes with unique properties.
Pyrococcus horikoshii is a hyperthermophilic archaeon known for its robust enzymes.

Purpose of the Study:

To identify and characterize a novel protein from Pyrococcus horikoshii with potential enzymatic activity.
To investigate the biochemical properties, including substrate specificity and optimal conditions, of the expressed protein.

Main Methods:

Bioinformatic analysis of Pyrococcus horikoshii genome to identify potential enzyme-encoding genes.
Cloning and expression of the identified gene in Escherichia coli.
Biochemical assays to determine enzyme activity, stability, and cofactor requirements.

Main Results:

An open reading frame encoding a 332-amino acid protein with homology to known peptidases was identified.
The expressed protein exhibited significant aminopeptidase activity, cleaving N-terminal amino acids from various peptide substrates.
The enzyme demonstrated remarkable thermostability, remaining active at temperatures above 90°C, with optimal activity at this temperature. Cobalt ions were essential for activity, while calcium ions were not.

Conclusions:

A novel, highly thermostable aminopeptidase was successfully characterized from Pyrococcus horikoshii.
This enzyme's ability to function at extreme temperatures and cleave N-terminal residues makes it a valuable tool for high-temperature peptide analysis, particularly for removing N(alpha)-acylated residues.