Functional mononuclear molybdenum enzymes: challenges and triumphs in molecular cloning, expression, and isolation
| Autor: | Breeanna Mintmier, Samih Nassif, Partha Basu, John F. Stolz |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
inorganic chemicals
Iron-Sulfur Proteins Xanthine Oxidase Heterologous chemistry.chemical_element Context (language use) Molecular cloning 010402 general chemistry 01 natural sciences Biochemistry Cofactor Inorganic Chemistry chemistry.chemical_compound Metalloproteins Pterin Cloning Molecular chemistry.chemical_classification Molybdenum biology Molecular Structure 010405 organic chemistry Sulfite Oxidase 0104 chemical sciences Enzyme chemistry biology.protein Molybdenum cofactor Oxidoreductases |
| Zdroj: | Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 25(4) |
| ISSN: | 1432-1327 |
| Popis: | Mononuclear molybdenum enzymes catalyze a variety of reactions that are essential in the cycling of nitrogen, carbon, arsenic, and sulfur. For decades, the structure and function of these crucial enzymes have been investigated to develop a fundamental knowledge for this vast family of enzymes and the chemistries they carry out. Therefore, obtaining abundant quantities of active enzyme is necessary for exploring this family's biochemical capability. This mini-review summarizes the methods for overexpressing mononuclear molybdenum enzymes in the context of the challenges encountered in the process. Effective methods for molybdenum cofactor synthesis and incorporation, optimization of expression conditions, improving isolation of active vs. inactive enzyme, incorporation of additional prosthetic groups, and inclusion of redox enzyme maturation protein chaperones are discussed in relation to the current molybdenum enzyme literature. This article summarizes the heterologous and homologous expression studies providing underlying patterns and potential future directions. |
| Databáze: | OpenAIRE |
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