Structural Basis of Substrate Conversion in a New Aromatic Peroxygenase
| Autor: | René Ullrich, Glenn Gröbe, Dietmar A. Plattner, Eric Strittmatter, Marek J. Pecyna, Klaus Piontek, Martin Kluge, Martin Hofrichter, Katrin Scheibner |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Hemeprotein biology 010405 organic chemistry Chemistry Stereochemistry Substrate (chemistry) Cell Biology 01 natural sciences Biochemistry 0104 chemical sciences 03 medical and health sciences chemistry.chemical_compound Oxidoreductase Unspecific peroxygenase biology.protein Organic synthesis Molecular Biology Heme Mixed Function Oxygenases 030304 developmental biology Peroxidase |
| Zdroj: | Journal of Biological Chemistry. 288:34767-34776 |
| ISSN: | 0021-9258 |
| Popis: | Aromatic peroxygenases (APOs) represent a unique oxidoreductase sub-subclass of heme proteins with peroxygenase and peroxidase activity and were thus recently assigned a distinct EC classification (EC 1.11.2.1). They catalyze, inter alia, oxyfunctionalization reactions of aromatic and aliphatic hydrocarbons with remarkable regio- and stereoselectivities. When compared with cytochrome P450, APOs appear to be the choice enzymes for oxyfunctionalizations in organic synthesis due to their independence from a cellular environment and their greater chemical versatility. Here, the first two crystal structures of a heavily glycosylated fungal aromatic peroxygenase (AaeAPO) are described. They reveal different pH-dependent ligand binding modes. We model the fitting of various substrates in AaeAPO, illustrating the way the enzyme oxygenates polycyclic aromatic hydrocarbons. Spatial restrictions by a phenylalanine pentad in the active-site environment govern substrate specificity in AaeAPO. |
| Databáze: | OpenAIRE |
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