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Cloning of a novel O-methyltransferase from Camellia sinensis and synthesis of o-methylated EGCG and evaluation of their bioactivity.
J Agric Food Chem. 2010 Jun 23; 58(12):7196-201.JA

Abstract

The gene of a novel O-methyltransferase was isolated from tea cultivars (Camellia sinensis L.). Using the recombinant enzyme, O-methylated (-)-epigallocatechin-3-O-gallate (EGCG) in all cases were synthesized. EGCG and the synthesized O-methylated EGCGs including (-)-epigallocatechin-3-O-(3-O-methyl)-gallate (EGCG3''Me), (-)-epigallocatechin-3-O- (4-O-methyl)-gallate(EGCG4''Me), (-)-epigallocatechin-3-O-(3,5-O-dimethyl)-gallate (EGCG3'',5''diMe), and (-)-3-O-methyl-epigallocatechin-3-O-(3,5-O-dimethyl)-gallate (EGCG3',3'',5''triMe) were assayed using the 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging assay and antibacterial activity. EGCG was the most effective of the O-methylated EGCGs. The antiallergic effects of EGCG and the other O-methylated EGCGs were measured by conducting histamine release assays using bone marrow-derived mouse mast cells, and the order of potency was EGCG3',3'',5''triMe = EGCG3'',5''diMe > EGCG3''Me > EGCG. These results indicated that reducing the number of hydroxyl groups decreases the effectiveness of DPPH radical scavenging and antibacterial activity. In contrast, the inhibition of histamine release was potentiated by an increase in the number of methyl groups in EGCG, especially in the galloyl moiety.

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Publisher Full Text (DOI)

Authors+Show Affiliations

Kirita M
Research Laboratories for Fundamental Technology of Food, Asahi Breweries Limited, Moriya-shi, Ibaraki, Japan. masanobu.kirita@asahibeer.co.jp
Honma D
No affiliation info available
Tanaka Y
No affiliation info available
Usui S
No affiliation info available
Shoji T
No affiliation info available
Sami M
No affiliation info available
Yokota T
No affiliation info available
Tagashira M
No affiliation info available
Muranaka A
No affiliation info available
Uchiyama M
No affiliation info available
Kanda T
No affiliation info available
Maeda-Yamamoto M
No affiliation info available

MeSH

Amino Acid SequenceAnimalsAnti-Allergic AgentsAnti-Bacterial AgentsBone Marrow CellsCamellia sinensisCatechinCloning, MolecularFree Radical ScavengersHistamine ReleaseMiceMolecular Sequence DataPlant ProteinsProtein O-MethyltransferaseSequence Alignment

Pub Type(s)

Journal Article

Language

eng

PubMed ID

20476742

Citation

Kirita, Masanobu, et al. "Cloning of a Novel O-methyltransferase From Camellia Sinensis and Synthesis of O-methylated EGCG and Evaluation of Their Bioactivity." Journal of Agricultural and Food Chemistry, vol. 58, no. 12, 2010, pp. 7196-201.
Kirita M, Honma D, Tanaka Y, et al. Cloning of a novel O-methyltransferase from Camellia sinensis and synthesis of o-methylated EGCG and evaluation of their bioactivity. J Agric Food Chem. 2010;58(12):7196-201.
Kirita, M., Honma, D., Tanaka, Y., Usui, S., Shoji, T., Sami, M., Yokota, T., Tagashira, M., Muranaka, A., Uchiyama, M., Kanda, T., & Maeda-Yamamoto, M. (2010). Cloning of a novel O-methyltransferase from Camellia sinensis and synthesis of o-methylated EGCG and evaluation of their bioactivity. Journal of Agricultural and Food Chemistry, 58(12), 7196-201. https://doi.org/10.1021/jf100493s
Kirita M, et al. Cloning of a Novel O-methyltransferase From Camellia Sinensis and Synthesis of O-methylated EGCG and Evaluation of Their Bioactivity. J Agric Food Chem. 2010 Jun 23;58(12):7196-201. PubMed PMID: 20476742.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cloning of a novel O-methyltransferase from Camellia sinensis and synthesis of o-methylated EGCG and evaluation of their bioactivity. AU - Kirita,Masanobu, AU - Honma,Daiki, AU - Tanaka,Yoshihisa, AU - Usui,Shinya, AU - Shoji,Toshihiko, AU - Sami,Manabu, AU - Yokota,Toyokazu, AU - Tagashira,Motoyuki, AU - Muranaka,Atsuya, AU - Uchiyama,Masanobu, AU - Kanda,Tomomasa, AU - Maeda-Yamamoto,Mari, PY - 2010/5/19/entrez PY - 2010/5/19/pubmed PY - 2010/10/6/medline SP - 7196 EP - 201 JF - Journal of agricultural and food chemistry JO - J Agric Food Chem VL - 58 IS - 12 N2 - The gene of a novel O-methyltransferase was isolated from tea cultivars (Camellia sinensis L.). Using the recombinant enzyme, O-methylated (-)-epigallocatechin-3-O-gallate (EGCG) in all cases were synthesized. EGCG and the synthesized O-methylated EGCGs including (-)-epigallocatechin-3-O-(3-O-methyl)-gallate (EGCG3''Me), (-)-epigallocatechin-3-O- (4-O-methyl)-gallate(EGCG4''Me), (-)-epigallocatechin-3-O-(3,5-O-dimethyl)-gallate (EGCG3'',5''diMe), and (-)-3-O-methyl-epigallocatechin-3-O-(3,5-O-dimethyl)-gallate (EGCG3',3'',5''triMe) were assayed using the 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging assay and antibacterial activity. EGCG was the most effective of the O-methylated EGCGs. The antiallergic effects of EGCG and the other O-methylated EGCGs were measured by conducting histamine release assays using bone marrow-derived mouse mast cells, and the order of potency was EGCG3',3'',5''triMe = EGCG3'',5''diMe > EGCG3''Me > EGCG. These results indicated that reducing the number of hydroxyl groups decreases the effectiveness of DPPH radical scavenging and antibacterial activity. In contrast, the inhibition of histamine release was potentiated by an increase in the number of methyl groups in EGCG, especially in the galloyl moiety. SN - 1520-5118 UR - https://www.unboundmedicine.com/medline/citation/20476742/Cloning_of_a_novel_O_methyltransferase_from_Camellia_sinensis_and_synthesis_of_o_methylated_EGCG_and_evaluation_of_their_bioactivity_ L2 - https://doi.org/10.1021/jf100493s DB - PRIME DP - Unbound Medicine ER -