1FOH
PHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUM
Summary for 1FOH
| Entry DOI | 10.2210/pdb1foh/pdb |
| Descriptor | PHENOL HYDROXYLASE, FLAVIN-ADENINE DINUCLEOTIDE, PHENOL, ... (4 entities in total) |
| Functional Keywords | flavin, phenol hydroxylase, monooxygenase, oxidoreductase |
| Biological source | Trichosporon cutaneum |
| Cellular location | Cytoplasm: P15245 |
| Total number of polymer chains | 4 |
| Total formula weight | 304309.21 |
| Authors | Enroth, C.,Neujahr, H.,Schneider, G.,Lindqvist, Y. (deposition date: 1998-03-26, release date: 1998-06-17, Last modification date: 2024-02-07) |
| Primary citation | Enroth, C.,Neujahr, H.,Schneider, G.,Lindqvist, Y. The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis. Structure, 6:605-617, 1998 Cited by PubMed Abstract: The synthesis of phenolic compounds as by-products of industrial reactions poses a serious threat to the environment. Understanding the enzymatic reactions involved in the degradation and detoxification of these compounds is therefore of much interest. Soil-living yeasts use flavin adenine dinucleotide (FAD)-containing enzymes to hydroxylate phenols. This reaction initiates a metabolic sequence permitting utilisation of the aromatic compound as a source of carbon and energy. The phenol hydroxylase from Trichosporon cutaneum hydroxylates phenol to catechol. Phenol is the best substrate, but the enzyme also accepts simple hydroxyl-, amino-, halogen- or methyl-substituted phenols. PubMed: 9634698DOI: 10.1016/S0969-2126(98)00062-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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