羟基化
单加氧酶
化学
过氧化物
芳构化
立体化学
过氧化物酶
基质(水族馆)
细胞色素P450
生物化学
酶
有机化学
生物
催化作用
生态学
作者
Martin Hofrichter,Harald Kellner,Robert Herzog,Alexander Karich,Jan Kiebist,Katrin Scheibner,René Ullrich
出处
期刊:Antioxidants
[MDPI AG]
日期:2022-01-14
卷期号:11 (1): 163-163
被引量:22
标识
DOI:10.3390/antiox11010163
摘要
Unspecific peroxygenases (UPOs), whose sequences can be found in the genomes of thousands of filamentous fungi, many yeasts and certain fungus-like protists, are fascinating biocatalysts that transfer peroxide-borne oxygen (from H2O2 or R-OOH) with high efficiency to a wide range of organic substrates, including less or unactivated carbons and heteroatoms. A twice-proline-flanked cysteine (PCP motif) typically ligates the heme that forms the heart of the active site of UPOs and enables various types of relevant oxygenation reactions (hydroxylation, epoxidation, subsequent dealkylations, deacylation, or aromatization) together with less specific one-electron oxidations (e.g., phenoxy radical formation). In consequence, the substrate portfolio of a UPO enzyme always combines prototypical monooxygenase and peroxidase activities. Here, we briefly review nearly 20 years of peroxygenase research, considering basic mechanistic, molecular, phylogenetic, and biotechnological aspects.
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