7AWV
Azoreductase (AzoRo) from Rhodococcus opacus 1CP
Summary for 7AWV
| Entry DOI | 10.2210/pdb7awv/pdb |
| Descriptor | FMN-dependent NADH-azoreductase, FLAVIN MONONUCLEOTIDE, ISOPROPYL ALCOHOL, ... (5 entities in total) |
| Functional Keywords | azoreductase; actinobacterium; dye degradation; nadh-quinone oxido-reductase, oxidoreductase |
| Biological source | Rhodococcus opacus |
| Total number of polymer chains | 2 |
| Total formula weight | 47317.47 |
| Authors | Bento, I.,Ngo, A.,Qi, J.,Juric, C.,Tischler, D. (deposition date: 2020-11-09, release date: 2022-02-02, Last modification date: 2024-05-01) |
| Primary citation | Ngo, A.C.R.,Qi, J.,Juric, C.,Bento, I.,Tischler, D. Identification of molecular basis that underlie enzymatic specificity of AzoRo from Rhodococcus opacus 1CP: A potential NADH:quinone oxidoreductase. Arch.Biochem.Biophys., 717:109123-109123, 2022 Cited by PubMed Abstract: Azo dyes are important to various industries such as textile industries. However, these dyes are known to comprise toxic, mutagenic, and carcinogenic representatives. Several approaches have already been employed to mitigate the problem such as the use of enzymes. Azoreductases have been well-studied in its capability to reduce azo dyes. AzoRo from Rhodococcus opacus 1CP has been found to be accepting only methyl red as a substrate, surmising that the enzyme may have a narrow active site. To determine the active site configuration of AzoRo at atomic level and identify the key residues involved in substrate binding and enzyme specificity, we have determined the crystal structure of holo-AzoRo and employed a rational design approach to generate AzoRo variants. The results reported here show that AzoRo has a different configuration of the active site when compared with other bacterial NAD(P)H azoreductases, having other key residues playing a role in the substrate binding and restricting the enzyme activity towards different azo dyes. Moreover, it was observed that AzoRo has only about 50% coupling yield to methyl red and p-benzoquinone - giving rise to the possibility that NADH oxidation still occurs even during catalysis. Results also showed that AzoRo is more active and more efficient towards quinones (about four times higher than methyl red). PubMed: 35051387DOI: 10.1016/j.abb.2022.109123 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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