Structural basis of substrate conversion in a new aromatic peroxygenase: cytochrome P450 functionality with benefits

  • 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.

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Author: Klaus Piontek, Eric Strittmatter, René UllrichORCiD, Glenn Gröbe, Marek J. Pecyna, Martin Kluge, Katrin Scheibner, Martin HofrichterORCiD, Dietmar A. Plattner
DOI:https://doi.org/10.1074/jbc.M113.514521
ISSN:1083-351X
Title of the source (English):The Journal of Biological Chemistry
Document Type:Scientific journal article peer-reviewed
Language:English
Year of publication:2013
Tag:Cytochrome P450; Fungi; Glycoprotein; Oxyfunctionalization; Peroxygenase; Polycyclic Aromatic Hydrocarbons
Issue number:288
First Page:34767
Last Page:34776
Faculty/Chair:Fakultät 2 Umwelt und Naturwissenschaften / FG Enzymtechnologie
Institution name at the time of publication:Fakultät für Naturwissenschaften (eHL) / Prof. Enzymtechnologie
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