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Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus furiosus

J M Muir¹, R J Russell, D W Hough

¹School of Biology and Biochemistry, University of Bath, UK.

Protein Engineering

|June 1, 1995

Summary

The citrate synthase gene from the hyperthermophilic Archaeon Pyrococcus furiosus was cloned and sequenced. The enzyme was over-expressed and characterized, revealing its hyperthermostable properties.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Citrate synthase is a key enzyme in the citric acid cycle.
Understanding hyperthermophilic enzymes provides insights into protein stability at extreme temperatures.

Purpose of the Study:

To clone, sequence, and characterize the citrate synthase gene and enzyme from Pyrococcus furiosus.
To compare the P. furiosus citrate synthase phylogenetically and structurally with other known citrate synthases.

Main Methods:

Gene cloning and sequencing of Pyrococcus furiosus citrate synthase.
Over-expression of the enzyme in Escherichia coli.
Enzyme characterization (kinetic, oligomeric, hyperthermostability).
Phylogenetic analysis and homology modeling based on structural alignment.

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Main Results:

The citrate synthase gene from P. furiosus was successfully cloned and sequenced.
The recombinant enzyme exhibited hyperthermostable properties and was enzymatically active.
Phylogenetic analysis placed P. furiosus citrate synthase within the archaeal lineage.
A homology model of P. furiosus citrate synthase was generated.

Conclusions:

The P. furiosus citrate synthase is a hyperthermostable enzyme with unique properties.
Structural and phylogenetic comparisons offer insights into enzyme evolution and adaptation to extreme environments.