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

Autor: Kyung Ha Lee, Tae Hoon Lee, Sang-Won Lee, Hyo Jeong Nam, Jae Chul Lee, Hye Lin Park, Man-Ho Cho, Seong Hee Bhoo, Jeong Min Lee
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Naringenin
PfOMT3
Pharmaceutical Science
01 natural sciences
Article
Substrate Specificity
Analytical Chemistry
Sakuranetin
lcsh:QD241-441
03 medical and health sciences
chemistry.chemical_compound
perilla
flavonoid 7-O-methyltransferase
lcsh:Organic chemistry
Drug Discovery
Amino Acid Sequence
7-methoxyflavonoid
Physical and Theoretical Chemistry
Chromatography
High Pressure Liquid
Phylogeny
030304 developmental biology
0303 health sciences
biology
Phenylpropanoid
010405 organic chemistry
Organic Chemistry
fungi
food and beverages
Methyltransferases
Eriodictyol
Flavones
O-methyltransferase
Recombinant Proteins
0104 chemical sciences
Plant Leaves
Kinetics
chemistry
Biochemistry
Chemistry (miscellaneous)
Apigenin
biology.protein
Molecular Medicine
biotransformation
Kaempferol
Luteolin
Biotechnology
Zdroj: Molecules
Volume 25
Issue 19
Molecules, Vol 25, Iss 4455, p 4455 (2020)
ISSN: 1420-3049
DOI: 10.3390/molecules25194455
Popis: 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.
Databáze: OpenAIRE
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