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Catalytically Perfect Enzymes

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.

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Related Experiment Video

Updated: Jan 5, 2026

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

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Correction to Directed Evolution of Split APEX2 Peroxidase

Yisu Han, Tess Caroline Branon, Jeffrey D Martell

ACS Chemical Biology

|October 29, 2019

Summary

No abstract available in PubMed .

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