Washington: Chemists have engineered a synthetic version of a natural enzyme which had the same catalytic power as that of its counterpart. These designer enzymes could revolutionise areas like drug production, environmental chemistry and bioremediation.

Catalysts are molecules that speed up chemical reactions both in the industrial and biological processes, without being changed themselves.

"The Holy Grail of enzyme catalysis is the ability to design enzymes," said Arieh Warshel, professor of chemistry at University of Southern California and co-author of a new paper on the subject.

Different keys are not supposed to fit the same lock, but in biological systems, multiple versions of a catalyst all make a reaction go, according to the study that explained the phenomenon.

Since the early days of catalyst chemistry, scientists had championed the "lock and key" model, which held that a catalyst worked by exquisitely surrounding and matching the reacting system (the substrate).

Warshel's group has published several papers which theorised that a perfect physical fit between catalyst and substrate is not necessary.

"What really fits is the electrostatic interaction between the enzyme active site to the substrate charges at the so-called transition state, where the bonds are halfway to being broken," Warshel said.

If Warshel is correct, catalyst and substrate would be less like lock and key, and more like two magnets: As long the opposite poles could get close to each other, they would bind.

These findings are scheduled for online publication in PNAS Early Edition. IANS