Monooxygenation of aromatic compounds by flavin‐dependent monooxygenases

Chenprakhon, Pirom; Wongnate, Thanyaporn; Chaiyen, Pimchai

doi:10.1002/pro.3525

Cited by 79 publications

(66 citation statements)

References 150 publications

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“…Monooxygenation is the incorporation of one hydroxyl group (–OH) derived from molecular oxygen into organic compounds. Monooxygenases that catalyse monooxygenation are metal‐dependent, pterin‐dependent and flavin‐dependent enzymes (van Berkel et al ., ; Roberts and Fitzpatrick, ; Huijbers et al ., ; Romero et al ., ; Banerjee et al ., ; Chenprakhon et al ., ). For monooxygenation of halogenated aromatics, the majority of the reactions are catalysed by flavin‐dependent monooxygenases (Arora and Bae, ).…”

Section: The Middle Metabolic Pathways For Dehalogenation Of Halogenamentioning

confidence: 97%

“…Flavin‐dependent dehalogenases can be divided into two types: single‐ and two‐component flavin‐dependent monooxygenases. Generally, all steps of the single‐component monooxygenases are catalysed by one polypeptide which binds oxidized flavin (flavin ox ) as a cofactor (Ballou et al ., ; van Berkel et al ., ; Palfey and McDonald, ; Huijbers et al ., ; Chenprakhon et al ., ). In contrast, reactions of two‐component flavin‐dependent monooxygenases are carried out by a separate reductase and oxygenase.…”

Section: The Middle Metabolic Pathways For Dehalogenation Of Halogenamentioning

confidence: 97%

“…For the oxidative mode, it generally involves with oxygen incorporation via various pathways yielding hydroxylated aromatic products such as derivatives of catechol, hydroquinone or protocatechuate which also have low cellular toxicity and higher solubility than the original toxic substrates. The final stage (lower pathway) deals with ring‐cleavage reactions to convert aromatic into aliphatic molecules which can be further cleaved to form common metabolites of central metabolic pathways such as succinate, pyruvate, acetyl CoA, oxaloacetate and acetaldehyde (Commandeur and Parsons, ; Harwood and Parales, ; Fuchs et al ., ; Arora and Bae, ; Tinikul et al ., ; Chenprakhon et al ., ).…”

Section: Introductionmentioning

confidence: 97%

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Microbial degradation of halogenated aromatics: molecular mechanisms and enzymatic reactions

Pimviriyakul

Wongnate

Tinikul

et al. 2019

Microbial Biotechnology

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Summary Halogenated aromatics are used widely in various industrial, agricultural and household applications. However, due to their stability, most of these compounds persist for a long time, leading to accumulation in the environment. Biological degradation of halogenated aromatics provides sustainable, low‐cost and environmentally friendly technologies for removing these toxicants from the environment. This minireview discusses the molecular mechanisms of the enzymatic reactions for degrading halogenated aromatics which naturally occur in various microorganisms. In general, the biodegradation process (especially for aerobic degradation) can be divided into three main steps: upper, middle and lower metabolic pathways which successively convert the toxic halogenated aromatics to common metabolites in cells. The most difficult step in the degradation of halogenated aromatics is the dehalogenation step in the middle pathway. Although a variety of enzymes are involved in the degradation of halogenated aromatics, these various pathways all share the common feature of eventually generating metabolites for utilizing in the energy‐producing metabolic pathways in cells. An in‐depth understanding of how microbes employ various enzymes in biodegradation can lead to the development of new biotechnologies via enzyme/cell/metabolic engineering or synthetic biology for sustainable biodegradation processes.

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Section: The Middle Metabolic Pathways For Dehalogenation Of Halogenamentioning

confidence: 97%

Section: The Middle Metabolic Pathways For Dehalogenation Of Halogenamentioning

confidence: 97%

Section: Introductionmentioning

confidence: 97%

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Microbial degradation of halogenated aromatics: molecular mechanisms and enzymatic reactions

Pimviriyakul

Wongnate

Tinikul

et al. 2019

Microbial Biotechnology

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“…Our results indicate that in the absence of RslO2, its function can be substituted by a Flavin reductase, encoded in the genome of S. albus J1074. Flavin dependent monooxygenases represent a special group of tailoring enzymes [8]. They catalyze the activation of molecular oxygen in the presence of a reduced flavin-cofactor, leading to the incorporation of oxygen into a molecule.…”

Section: Rishirilide Production Is Not Strongly Affected By Deletionsmentioning

confidence: 99%

Early Steps in the Biosynthetic Pathway of Rishirilide B

et al. 2020

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The biological active compound rishirilide B is produced by Streptomyces bottropensis. The cosmid cos4 contains the complete rishirilide B biosynthesis gene cluster. Its heterologous expression in the host Streptomyces albus J1074 led to the production of rishirilide B as a major compound and to small amounts of rishirilide A, rishirilide D and lupinacidin A. In order to gain more insights into the biosynthesis, gene inactivation experiments and gene expression experiments were carried out. This study lays the focus on the functional elucidation of the genes involved in the early biosynthetic pathway. A total of eight genes were deleted and six gene cassettes were generated. Rishirilide production was not strongly affected by mutations in rslO2, rslO6 and rslH. The deletion of rslK4 and rslO3 led to the formation of polyketides with novel structures. These results indicated that RslK4 and RslO3 are involved in the generation or selection of the starter unit for rishirilide biosynthesis. In the rslO10 mutant strain, two novel compounds were detected, which were also produced by a strain containing solely the genes rslK1, rslK2, rslK3, rslK4, and rslA. rslO1 and rslO4 mutants predominately produce galvaquinones. Therefore, the ketoreductase RslO10 is involved in an early step of rishirilide biosynthesis and the oxygenases RslO1 and RslO4 are most probably acting on an anthracene moiety. This study led to the functional elucidation of several genes of the rishirilide pathway, including rslK4, which is involved in selecting the unusual starter unit for polyketide synthesis.Molecules 2020, 25, 1955 2 of 15 the initiation module, can be found, consisting of a ketosynthase, a malonyl CoA:ACP transferase and an acyl carrier protein (ACP). The initiation module selects the starter unit and catalyzes the first elongation of the growing polyketide, before the molecule is loaded onto the minPKS for further elongation reactions. Additional enzymes, like ketoreductases, cyclases and aromatases complement the minPKS and determine the folding of the respective polyketide [1]. The aromatic polyketide rishirilide B (Figure 1) was first discovered by Iwaki et al. in 1984. Rishirilide B was isolated from Streptomyces rishiriensis OFR-1056 in the course of screening for new α2-macroglobulin inhibitors [2]. This compound was also described as a product of S. olivaceus SCSIO T05, which also produced rishirilide C, lupinacidin A and galvaquinone A and B [3] (Figure 1). The biosynthetic gene cluster of this strain responsible for the formation of all four compounds was cloned and biosynthetic studies were performed [3]. S. bottropensis (formerly S. sp. Gö C4/4) also produces the compounds rishirilide A, B, D and lupinacidin A (Figure 1). The corresponding rishirilide biosynthetic gene cluster was cloned on a cosmid (cos4), which was subsequently expressed in the heterologous host S. albus J1074. Rishirilide B was produced as a major compound. Moreover, rishirilide A, D and lupinacidin A were also produced in small amounts [3] (Figure 1)....

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“…In the case of the two‐component flavin‐dependent monooxygenases, in general, the reduced flavin generated by a flavin reductase must be transferred to a corresponding monooxygenase to complete the hydroxylation reaction. Therefore, key biological processes such as catabolism, detoxification, biosynthesis, and light emission often involve coupled reductase‐ and monooxygenase‐catalyzed reactions …”

Section: Introductionmentioning

confidence: 99%

Creating Flavin Reductase Variants with Thermostable and Solvent‐Tolerant Properties by Rational‐Design Engineering

et al. 2020

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Scheme1.The C 1 -catalyzed reaction thatg enerates FMNH À for monooxygenase-catalyzed reactions.The NADH-regenerating systemm ightb e, for example, glucose/glucose dehydrogenase, glucose 6-phosphate/glucose 6phosphate dehydrogenase, [41,42] or formate/formate dehydrogenase. [43,44] The monooxygenases mightb e, for example, C 2 or bacterialluciferase. Figure 6. Distances between A58/P58 and I14:A )int he wild type, and B) in the A58P variant over 6nsM Ds imulation,a ttemperatures varying from 300-500 K. The interactions between A58/P58 of C) the wild type, and D) the A58P variant and other residues after 6-ns MD simulations.

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Monooxygenation of aromatic compounds by flavin‐dependent monooxygenases

Cited by 79 publications

References 150 publications

Microbial degradation of halogenated aromatics: molecular mechanisms and enzymatic reactions

Microbial degradation of halogenated aromatics: molecular mechanisms and enzymatic reactions

Early Steps in the Biosynthetic Pathway of Rishirilide B

Creating Flavin Reductase Variants with Thermostable and Solvent‐Tolerant Properties by Rational‐Design Engineering

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