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Biochemical Characterization of a Flavonoid O-methyltransferase from Perilla Leaves and Its Application in 7-Methoxyflavonoid Production

Methylation is a common structural modification that can alter and improve the biological activities of natural compounds. O-Methyltransferases (OMTs) catalyze the methylation of a wide array of secondary metabolites, including flavonoids, and are potentially useful tools for the biotechnological pr...

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Autores principales: Park, Hye Lin, Lee, Jae Chul, Lee, Kyungha, Lee, Jeong Min, Nam, Hyo Jeong, Bhoo, Seong Hee, Lee, Tae Hoon, Lee, Sang-Won, Cho, Man-Ho
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7583084/
https://www.ncbi.nlm.nih.gov/pubmed/32998370
http://dx.doi.org/10.3390/molecules25194455
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author Park, Hye Lin
Lee, Jae Chul
Lee, Kyungha
Lee, Jeong Min
Nam, Hyo Jeong
Bhoo, Seong Hee
Lee, Tae Hoon
Lee, Sang-Won
Cho, Man-Ho
author_facet Park, Hye Lin
Lee, Jae Chul
Lee, Kyungha
Lee, Jeong Min
Nam, Hyo Jeong
Bhoo, Seong Hee
Lee, Tae Hoon
Lee, Sang-Won
Cho, Man-Ho
author_sort Park, Hye Lin
collection PubMed
description Methylation is a common structural modification that can alter and improve the biological activities of natural compounds. O-Methyltransferases (OMTs) catalyze the methylation of a wide array of secondary metabolites, including flavonoids, and are potentially useful tools for the biotechnological production of valuable natural products. An OMT gene (PfOMT3) was isolated from perilla leaves as a putative flavonoid OMT (FOMT). Phylogenetic analysis and sequence comparisons showed that PfOMT3 is a class II OMT. Recombinant PfOMT3 catalyzed the methylation of flavonoid substrates, whereas no methylated product was detected in PfOMT3 reactions with phenylpropanoid substrates. Structural analyses of the methylation products revealed that PfOMT3 regiospecifically transfers a methyl group to the 7-OH of flavonoids. These results indicate that PfOMT3 is an FOMT that catalyzes the 7-O-methylation of flavonoids. PfOMT3 methylated diverse flavonoids regardless of their backbone structure. Chrysin, naringenin and apigenin were found to be the preferred substrates of PfOMT3. Recombinant PfOMT3 showed moderate OMT activity toward eriodictyol, luteolin and kaempferol. To assess the biotechnological potential of PfOMT3, the biotransformation of flavonoids was performed using PfOMT3-transformed Escherichia coli. Naringenin and kaempferol were successfully bioconverted to the 7-methylated products sakuranetin and rhamnocitrin, respectively, by E. coli harboring PfOMT3.
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spelling pubmed-75830842020-10-28 Biochemical Characterization of a Flavonoid O-methyltransferase from Perilla Leaves and Its Application in 7-Methoxyflavonoid Production Park, Hye Lin Lee, Jae Chul Lee, Kyungha Lee, Jeong Min Nam, Hyo Jeong Bhoo, Seong Hee Lee, Tae Hoon Lee, Sang-Won Cho, Man-Ho Molecules Article Methylation is a common structural modification that can alter and improve the biological activities of natural compounds. O-Methyltransferases (OMTs) catalyze the methylation of a wide array of secondary metabolites, including flavonoids, and are potentially useful tools for the biotechnological production of valuable natural products. An OMT gene (PfOMT3) was isolated from perilla leaves as a putative flavonoid OMT (FOMT). Phylogenetic analysis and sequence comparisons showed that PfOMT3 is a class II OMT. Recombinant PfOMT3 catalyzed the methylation of flavonoid substrates, whereas no methylated product was detected in PfOMT3 reactions with phenylpropanoid substrates. Structural analyses of the methylation products revealed that PfOMT3 regiospecifically transfers a methyl group to the 7-OH of flavonoids. These results indicate that PfOMT3 is an FOMT that catalyzes the 7-O-methylation of flavonoids. PfOMT3 methylated diverse flavonoids regardless of their backbone structure. Chrysin, naringenin and apigenin were found to be the preferred substrates of PfOMT3. Recombinant PfOMT3 showed moderate OMT activity toward eriodictyol, luteolin and kaempferol. To assess the biotechnological potential of PfOMT3, the biotransformation of flavonoids was performed using PfOMT3-transformed Escherichia coli. Naringenin and kaempferol were successfully bioconverted to the 7-methylated products sakuranetin and rhamnocitrin, respectively, by E. coli harboring PfOMT3. MDPI 2020-09-28 /pmc/articles/PMC7583084/ /pubmed/32998370 http://dx.doi.org/10.3390/molecules25194455 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Park, Hye Lin
Lee, Jae Chul
Lee, Kyungha
Lee, Jeong Min
Nam, Hyo Jeong
Bhoo, Seong Hee
Lee, Tae Hoon
Lee, Sang-Won
Cho, Man-Ho
Biochemical Characterization of a Flavonoid O-methyltransferase from Perilla Leaves and Its Application in 7-Methoxyflavonoid Production
title Biochemical Characterization of a Flavonoid O-methyltransferase from Perilla Leaves and Its Application in 7-Methoxyflavonoid Production
title_full Biochemical Characterization of a Flavonoid O-methyltransferase from Perilla Leaves and Its Application in 7-Methoxyflavonoid Production
title_fullStr Biochemical Characterization of a Flavonoid O-methyltransferase from Perilla Leaves and Its Application in 7-Methoxyflavonoid Production
title_full_unstemmed Biochemical Characterization of a Flavonoid O-methyltransferase from Perilla Leaves and Its Application in 7-Methoxyflavonoid Production
title_short Biochemical Characterization of a Flavonoid O-methyltransferase from Perilla Leaves and Its Application in 7-Methoxyflavonoid Production
title_sort biochemical characterization of a flavonoid o-methyltransferase from perilla leaves and its application in 7-methoxyflavonoid production
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7583084/
https://www.ncbi.nlm.nih.gov/pubmed/32998370
http://dx.doi.org/10.3390/molecules25194455
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