5i38 | pdb_00005i38

Crystal Structure of tyrosinase from Bacillus megaterium with inhibitor kojic acid in the active site

spinqualitylabelsall models 5i38, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5i38 is a 2 chain structure with sequence from Priestia megaterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: CU, KOJ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B2ZB02_PRIMG Publication Abstract from PubMed 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. The unravelling of the complex pattern of tyrosinase inhibition.,Deri B, Kanteev M, Goldfeder M, Lecina D, Guallar V, Adir N, Fishman A Sci Rep. 2016 Oct 11;6:34993. doi: 10.1038/srep34993. PMID:27725765 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tyrosinase 3D structures

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