By a News Reporter-Staff News Editor at Life Science Weekly -- Research findings on Proteins are discussed in a new report. According to news reporting out of Senftenberg, Germany, by NewsRx editors, research stated, "Aromatic peroxygenases (APOs) are the missing link between heme peroxidases and P450-monooxygenases. Based on two crystal structures the substrate conversion of APOs is elucidated."
Our news journalists obtained a quote from the research from the University of Applied Sciences, "The specific design of the heme cavity and the distal heme access channel govern substrate specificity. APOs can be utilized in biotechnology and organic synthesis having significant advantages when compared with cytochrome P450 enzymes. 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 184.108.40.206). 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."
According to the news editors, the research concluded: "Spatial restrictions by a phenylalanine pentad in the active-site environment govern substrate specificity in AaeAPO."
For more information on this research see: Structural Basis of Substrate Conversion in a New Aromatic Peroxygenase CYTOCHROME P450 FUNCTIONALITY WITH BENEFITS. Journal of Biological Chemistry, 2013;288(48):34767-34776. Journal of Biological Chemistry can be contacted at: Amer Soc Biochemistry Molecular Biology Inc, 9650 Rockville Pike, Bethesda, MD 20814-3996, USA. (American Society for Biochemistry and Molecular Biology - www.asbmb.org; Journal of Biological Chemistry - www.jbc.org/)
Our news journalists report that additional information may be obtained by contacting K. Piontek, Lausitz Univ Appl Sci, Dept. of Biotechnol, Fac Nat Sci, D-01968 Senftenberg, Germany. Additional authors for this research include E. Strittmatter, R. Ullrich, G. Grobe, M.J. Pecyna, M. Kluge, K. Scheibner, M. Hofrichter and D.A. Plattner (see also Proteins).
Keywords for this news article include: Europe, Germany, Senftenberg, Cytochromes, Hemeproteins, Metalloporphyrins
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