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Recombinant Proteins
Recombinant Human AASS (argininosuccinate synthase) is a key enzyme involved in the urea cycle, which is responsible for the detoxification of ammonia in the body. This enzyme is encoded by the ASS1 gene and is essential for the production of arginine, an important amino acid for protein synthesis. In recent years, recombinant human AASS has been extensively studied and has shown promising potential for therapeutic applications. In this article, we will discuss the structure, activity, and potential applications of recombinant human AASS.
Recombinant human AASS is a homotetrameric protein, meaning it is composed of four identical subunits. Each subunit consists of 412 amino acids and has a molecular weight of approximately 46 kDa. The crystal structure of recombinant human AASS has been determined and it shows a highly conserved fold with other members of the argininosuccinate synthase family. The active site of the enzyme is located at the interface of two subunits and contains a highly reactive cysteine residue that is essential for catalysis.
The main function of recombinant human AASS is to catalyze the conversion of citrulline and aspartate into argininosuccinate, a key step in the urea cycle. This reaction is crucial for the removal of excess ammonia from the body. In addition, recombinant human AASS has been shown to have a role in the biosynthesis of arginine, which is important for various physiological processes such as cell growth, wound healing, and immune function.
Recombinant human AASS has been extensively studied in terms of its enzymatic activity and has been found to have a high affinity for its substrates, citrulline and aspartate. It has also been shown to have a high turnover rate, making it an efficient catalyst for the urea cycle. Moreover, recombinant human AASS has been found to be stable and active at a wide range of temperatures and pH, making it suitable for industrial applications.
Recombinant human AASS has shown potential for therapeutic applications, particularly in the treatment of urea cycle disorders (UCD). UCDs are a group of rare genetic disorders that result in the accumulation of ammonia in the body, leading to neurological damage and other serious health complications. Currently, the main treatment for UCDs is a protein-restricted diet and medication, but these treatments are not always effective and can have significant side effects. Recombinant human AASS has the potential to be used as a replacement therapy for UCDs, as it can provide the missing enzyme and help reduce ammonia levels in the body.
In addition, recombinant human AASS has also been investigated for its potential in cancer therapy. Cancer cells have a high demand for arginine, and recombinant human AASS has been shown to inhibit the growth of cancer cells by depleting their arginine supply. Furthermore, studies have shown that recombinant human AASS can enhance the effectiveness of certain chemotherapeutic drugs, making it a potential adjuvant therapy for cancer treatment.
Recombinant Human AASS is a key enzyme involved in the urea cycle and has shown promising potential for therapeutic applications. Its structure and activity have been extensively studied, and it has been found to be stable and efficient in catalyzing the conversion of citrulline and aspartate into argininosuccinate. Its potential applications include the treatment of urea cycle disorders and cancer therapy. Further research and development of recombinant human AASS may lead to improved treatments for these conditions and other potential applications.
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