5I3A
Crystal Structure of tyrosinase from Bacillus megaterium with configuration A of hydroquinone inhibitor in the active site
Summary for 5I3A
| Entry DOI | 10.2210/pdb5i3a/pdb |
| Descriptor | Tyrosinase, ZINC ION, benzene-1,4-diol, ... (4 entities in total) |
| Functional Keywords | di-copper oxidase, oxidoreductase |
| Biological source | Bacillus megaterium |
| Total number of polymer chains | 2 |
| Total formula weight | 67125.80 |
| Authors | Kanteev, M.,Deri, B.,Adir, N.,Fishman, A. (deposition date: 2016-02-10, release date: 2016-10-12, Last modification date: 2024-01-10) |
| Primary citation | Deri, B.,Kanteev, M.,Goldfeder, M.,Lecina, D.,Guallar, V.,Adir, N.,Fishman, A. The unravelling of the complex pattern of tyrosinase inhibition. Sci Rep, 6:34993-34993, 2016 Cited by PubMed Abstract: Tyrosinases are responsible for melanin formation in all life domains. Tyrosinase inhibitors are used for the prevention of severe skin diseases, in skin-whitening creams and to avoid fruit browning, however continued use of many such inhibitors is considered unsafe. In this study we provide conclusive evidence of the inhibition mechanism of two well studied tyrosinase inhibitors, KA (kojic acid) and HQ (hydroquinone), which are extensively used in hyperpigmentation treatment. KA is reported in the literature with contradicting inhibition mechanisms, while HQ is described as both a tyrosinase inhibitor and a substrate. By visualization of KA and HQ in the active site of TyrBm crystals, together with molecular modeling, binding constant analysis and kinetic experiments, we have elucidated their mechanisms of inhibition, which was ambiguous for both inhibitors. We confirm that while KA acts as a mixed inhibitor, HQ can act both as a TyrBm substrate and as an inhibitor. PubMed: 27725765DOI: 10.1038/srep34993 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
