Download MendeleyThe 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.
Enroth, C., Neujahr, H., Schneider, G., Lindqvist, Y.(1998) Structure 6: 605-617
- PubMed: 9634698
- DOI: https://doi.org/10.1016/s0969-2126(98)00062-8
- Primary Citation of Related Structures:
1FOH - 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.
Organizational Affiliation:
Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.
