Publication: Phenolic hydroxylases
Issued Date
2020-01-01
Resource Type
ISSN
18746047
Other identifier(s)
2-s2.0-85088149485
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Mahidol University
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SCOPUS
Bibliographic Citation
Enzymes. (2020)
Suggested Citation
Pirom Chenprakhon, Panu Pimviriyakul, Chanakan Tongsook, Pimchai Chaiyen Phenolic hydroxylases. Enzymes. (2020). doi:10.1016/bs.enz.2020.05.008 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/57756
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Title
Phenolic hydroxylases
Abstract
© 2020 Elsevier Inc. Many flavin-dependent phenolic hydroxylases (monooxygenases) have been extensively investigated. Their crystal structures and reaction mechanisms are well understood. These enzymes belong to groups A and D of the flavin-dependent monooxygenases and can be classified as single-component and two-component flavin-dependent monooxygenases. The insertion of molecular oxygen into the substrates catalyzed by these enzymes is beneficial for modifying the biological properties of phenolic compounds and their derivatives. This chapter provides an in-depth discussion of the structural features of single-component and two-component flavin-dependent phenolic hydroxylases. The reaction mechanisms of selected enzymes, including 3-hydroxy-benzoate 4-hydroxylase (PHBH) and 3-hydroxy-benzoate 6-hydroxylase as representatives of single-component enzymes and 3-hydroxyphenylacetate 4-hydroxylase (HPAH) as a representative of two-component enzymes, are discussed in detail. This chapter comprises the following four main parts: general reaction, structures, reaction mechanisms, and enzyme engineering for biocatalytic applications. Enzymes belonging to the same group catalyze similar reactions but have different unique structural features to control their reactivity to substrates and the formation and stabilization of C4a-hydroperoxyflavin. Protein engineering has been employed to improve the ability to use these enzymes to synthesize valuable compounds. A thorough understanding of the structural and mechanistic features controlling enzyme reactivity is useful for enzyme redesign and enzyme engineering for future biocatalytic applications.