Recombinant Human ECI2, N-His

Description of Recombinant Human ECI2, N-His

Introduction

Recombinant Human ECI2, N-His is a protein that has gained significant attention in the field of drug discovery due to its potential as a drug target. This protein is a member of the enoyl-CoA delta isomerase family and plays a crucial role in fatty acid metabolism. In this article, we will discuss the structure, activity, and potential applications of Recombinant Human ECI2, N-His in drug development.

Structure of Recombinant Human ECI2, N-His

The Recombinant Human ECI2, N-His protein is a 27 kDa protein that is composed of 240 amino acids. It is encoded by the ECI2 gene located on chromosome 6 in humans. The protein consists of two domains, an N-terminal domain and a C-terminal domain. The N-terminal domain contains the active site of the protein, while the C-terminal domain is involved in protein-protein interactions.

The crystal structure of Recombinant Human ECI2, N-His has been determined, and it is found to have a similar structure to other members of the enoyl-CoA delta isomerase family. It adopts a beta-barrel fold with a central core of eight beta-strands surrounded by eight alpha-helices. This structure is essential for the protein’s function as it allows it to bind with its substrates and carry out its enzymatic activity.

Activity of this protein

Recombinant Human ECI2, N-His is an enzyme that plays a crucial role in fatty acid metabolism. It catalyzes the isomerization of trans-2,3-enoyl-CoA to cis-2,3-enoyl-CoA, an essential step in the beta-oxidation of fatty acids. This process is crucial for the production of energy in the form of ATP. Defects in this enzyme have been linked to various metabolic disorders, making it a potential drug target.

The enzymatic activity of Recombinant Human ECI2, N-His is dependent on the presence of a divalent metal ion, typically magnesium or manganese. This metal ion is essential for stabilizing the transition state during the isomerization reaction. In addition, the N-terminal domain of the protein contains a catalytic triad of amino acids, which is responsible for the enzyme’s activity.

Potential Applications in Drug Development

Due to its crucial role in fatty acid metabolism, Recombinant Human ECI2, N-His has been identified as a potential drug target for various metabolic disorders. Mutations in the ECI2 gene have been linked to disorders such as type 2 diabetes, obesity, and metabolic syndrome. Inhibiting the activity of this enzyme could potentially lead to the development of new therapeutics for these diseases.

In addition to its role in metabolic disorders, Recombinant Human ECI2, N-His has also been studied as a potential target in cancer therapy. Studies have shown that this enzyme is overexpressed in certain types of cancer, and inhibiting its activity can lead to cancer cell death. This makes it a promising target for the development of new cancer treatments.

Furthermore, Recombinant Human ECI2, N-His has also been investigated as a potential target for the treatment of parasitic infections. The enzyme is essential for the survival of parasites such as Plasmodium falciparum, the causative agent of malaria. Inhibiting its activity could potentially lead to the development of new antimalarial drugs.

Conclusion

In summary, Recombinant Human ECI2, N-His is a 27 kDa protein that plays a crucial role in fatty acid metabolism. Its structure, activity, and potential applications in drug development make it an attractive drug target for various diseases.