Recombinant Human BCO1, N-His

Description of Recombinant Human BCO1, N-His

Introduction

Recombinant Human BCO1, also known as beta-carotene oxygenase 1, is a protein that plays a crucial role in the metabolism of beta-carotene, a precursor of vitamin A. This enzyme is encoded by the BCO1 gene and is found in various tissues such as the liver, intestine, and adipose tissue. In this article, we will discuss the structure, activity, and application of recombinant Human BCO1.

Structure of Recombinant Human BCO1

The BCO1 gene is located on chromosome 16 in humans and contains 12 exons. The protein encoded by this gene is a member of the carotenoid oxygenase family and consists of 575 amino acids. The recombinant form of Human BCO1 is produced by expressing the BCO1 gene in a suitable host organism, such as E. coli or yeast. The resulting protein has a predicted molecular weight of approximately 64 kDa.

The crystal structure of recombinant Human BCO1 has been determined, revealing a homodimeric enzyme with each monomer consisting of two domains: an N-terminal beta-barrel domain and a C-terminal alpha-helical domain. The active site of the enzyme is located at the interface of these two domains and is composed of a non-heme iron atom coordinated by histidine, aspartate, and glutamate residues.

Activity of Recombinant Human BCO1

The main function of recombinant Human BCO1 is to convert beta-carotene into retinal, which is then further metabolized to retinol, the active form of vitamin A. This process is essential for maintaining adequate levels of vitamin A in the body, which is crucial for various physiological processes such as vision, immune function, and cell growth and differentiation.

The activity of recombinant Human BCO1 is dependent on several factors such as pH, temperature, and substrate concentration. The enzyme has been shown to have optimal activity at a pH of 6.0 and a temperature of 37°C. It also exhibits a preference for beta-carotene over other carotenoids such as lycopene and lutein.

Application of Recombinant Human BCO1

Recombinant Human BCO1 has a wide range of applications in the fields of nutrition, medicine, and biotechnology. One of the most significant applications of this enzyme is in the production of vitamin A supplements. By using recombinant BCO1, large quantities of retinol can be produced from beta-carotene, which is a more cost-effective and sustainable method compared to traditional chemical synthesis.

In addition to its role in vitamin A production, recombinant Human BCO1 has also been used in the development of functional foods. These are foods that have been fortified with specific nutrients to provide health benefits beyond basic nutrition. By incorporating recombinant BCO1 into food products, manufacturers can enhance the bioavailability of beta-carotene and promote its conversion to vitamin A in the body.

Furthermore, recombinant Human BCO1 has been studied for its potential therapeutic applications. Research has shown that mutations in the BCO1 gene can lead to a deficiency in vitamin A and may contribute to various health conditions such as night blindness, macular degeneration, and obesity. By understanding the structure and function of recombinant BCO1, scientists can develop targeted therapies to treat these diseases.

Conclusion

In summary, recombinant Human BCO1 is a crucial enzyme involved in the metabolism of beta-carotene and the production of vitamin A. Its structure, activity, and application have been extensively studied, and it has shown great potential in various fields. As research on this enzyme continues, we can expect to see even more innovative uses for recombinant Human BCO1 in the future.