Recombinant Human GLO1 Protein, N-His

Description of Recombinant Human GLO1 Protein, N-His

Introduction

Recombinant Human GLO1 Protein is a highly efficient and versatile enzyme that plays a crucial role in the detoxification of methylglyoxal, a toxic byproduct of glycolysis. This protein is produced through recombinant DNA technology, allowing for large-scale production and purification for various research and industrial applications. In this article, we will explore the structure, activity, and applications of Recombinant Human GLO1 Protein.

Structure of Recombinant Human GLO1 Protein

Recombinant Human GLO1 Protein is a homodimeric enzyme, meaning it is composed of two identical subunits. Each subunit consists of 184 amino acids and has a molecular weight of approximately 21 kDa. The protein is encoded by the GLO1 gene, located on chromosome 6 in humans.

The crystal structure of Recombinant Human GLO1 Protein has been determined, revealing a compact globular structure with a central β-sheet surrounded by α-helices. The active site of the enzyme is located at the interface between the two subunits, where it binds to its substrate, methylglyoxal.

Activity of Recombinant Human GLO1 Protein

Recombinant Human GLO1 Protein is a highly active enzyme that catalyzes the conversion of methylglyoxal to D-lactate. This reaction is essential for the detoxification of methylglyoxal, which is a potent glycating agent that can damage cellular proteins and DNA. GLO1 is the primary enzyme responsible for the removal of methylglyoxal in human cells, making it a crucial component of the body’s defense against oxidative stress.

The activity of Recombinant Human GLO1 Protein is dependent on the presence of a cofactor, glutathione. Glutathione acts as an electron donor, allowing GLO1 to efficiently convert methylglyoxal to D-lactate. This cofactor is essential for the proper functioning of GLO1 and is often included in the enzyme’s purification process to ensure maximum activity.

Applications of Recombinant Human GLO1 Protein

Recombinant Human GLO1 Protein has a wide range of applications in both research and industrial settings. One of its primary uses is in drug discovery and development, as GLO1 is a potential target for the treatment of various diseases, including diabetes, cancer, and neurodegenerative disorders. Recombinant Human GLO1 Protein can be used to screen and identify potential inhibitors of GLO1 activity, which can then be further developed into therapeutic agents.

In addition to drug discovery, Recombinant Human GLO1 Protein is also used in biochemical and biophysical studies to understand the structure and function of the enzyme. Its high activity and stability make it an ideal tool for studying the mechanism of GLO1 and its interactions with other molecules.

Furthermore, Recombinant Human GLO1 Protein has industrial applications in the production of food and beverages. Methylglyoxal is a byproduct of the Maillard reaction, which is responsible for the browning and flavor development in many foods. GLO1 can be used to remove excess methylglyoxal, preventing the formation of off-flavors and improving the overall quality of food products.

Conclusion

Recombinant Human GLO1 Protein is a highly efficient and versatile enzyme with a crucial role in cellular detoxification. Its structure, activity, and applications make it a valuable tool in various fields, including drug discovery, biochemical and biophysical studies, and food production. As research on GLO1 continues, the potential for this enzyme to be used in new and innovative ways is promising.