Publication: Monooxygenation of aromatic compounds by flavin-dependent monooxygenases
Issued Date
2019-01-01
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ISSN
1469896X
09618368
09618368
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2-s2.0-85058507217
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Mahidol University
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SCOPUS
Bibliographic Citation
Protein Science. Vol.28, No.1 (2019), 8-29
Suggested Citation
Pirom Chenprakhon, Thanyaporn Wongnate, Pimchai Chaiyen Monooxygenation of aromatic compounds by flavin-dependent monooxygenases. Protein Science. Vol.28, No.1 (2019), 8-29. doi:10.1002/pro.3525 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/50319
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Title
Monooxygenation of aromatic compounds by flavin-dependent monooxygenases
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Abstract
© 2018 The Protein Society Many flavoenzymes catalyze hydroxylation of aromatic compounds especially phenolic compounds have been isolated and characterized. These enzymes can be classified as either single-component or two-component flavin-dependent hydroxylases (monooxygenases). The hydroxylation reactions catalyzed by the enzymes in this group are useful for modifying the biological properties of phenolic compounds. This review aims to provide an in-depth discussion of the current mechanistic understanding of representative flavin-dependent monooxygenases including 3-hydroxy-benzoate 4-hydroxylase (PHBH, a single-component hydroxylase), 3-hydroxyphenylacetate 4-hydroxylase (HPAH, a two-component hydroxylase), and other monooxygenases which catalyze reactions in addition to hydroxylation, including 2-methyl-3-hydroxypyridine-5-carboxylate oxygenase (MHPCO, a single-component enzyme that catalyzes aromatic-ring cleavage), and HadA monooxygenase (a two-component enzyme that catalyzes additional group elimination reaction). These enzymes have different unique structural features which dictate their reactivity toward various substrates and influence their ability to stabilize flavin intermediates such as C4a-hydroperoxyflavin. Understanding the key catalytic residues and the active site environments important for governing enzyme reactivity will undoubtedly facilitate future work in enzyme engineering or enzyme redesign for the development of biocatalytic methods for the synthesis of valuable compounds.