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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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Updated: May 22, 2026

Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes

Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes

Published on: October 3, 2019

A highly efficient galactokinase from Bifidobacterium infantis with broad substrate specificity.

Lei Li¹, Yonghui Liu, Wenjun Wang

¹College of Pharmacy and State Key Laboratory of Medicinal Chemical Biology, Nankai University, Nankai District, Tianjin 300071, PR China.

Carbohydrate Research

|May 29, 2012

Summary

A new Bifidobacterium infantis galactokinase (BiGalK) enzyme is significantly more efficient at phosphorylating galactose than the E. coli version. This highly efficient BiGalK also acts on galacturonic acid, making it valuable for producing galactose-1-phosphate.

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Last Updated: May 22, 2026

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Anti-virulent Disruption of Pathogenic Biofilms using Engineered Quorum-quenching Lactonases

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Published on: January 1, 2016

Area of Science:

Enzymology
Biotechnology
Microbial Biochemistry

Background:

Galactokinase (GalK) enzymes are crucial for synthesizing sugar-1-phosphates.
Escherichia coli GalK is commonly used but has limitations in efficiency.
Exploring alternative GalK sources can lead to improved biochemical processes.

Purpose of the Study:

To clone and characterize a novel galactokinase from Bifidobacterium infantis (BiGalK).
To compare the enzymatic efficiency of BiGalK with established GalK enzymes.
To investigate the substrate specificity of BiGalK for potential biotechnological applications.

Main Methods:

Gene cloning and overexpression of Bifidobacterium infantis galactokinase.
Enzyme activity assays to determine kinetic parameters (kcat/Km) towards galactose.
Testing BiGalK activity against various sugar substrates and phosphate donors.

Main Results:

Recombinant BiGalK was successfully overexpressed with a yield exceeding 80 mg/L.
BiGalK demonstrated a kcat/Km value 296 times higher than E. coli GalK for galactose phosphorylation.
BiGalK exhibited novel activity towards galacturonic acid and broad substrate specificity.

Conclusions:

BiGalK is a highly efficient enzyme for galactose phosphorylation, surpassing E. coli GalK.
The unique substrate profile of BiGalK opens new avenues for synthesizing galactose-1-phosphate and derivatives.
BiGalK represents a promising biocatalyst for industrial-scale production of valuable sugar phosphates.