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한국식물학회 / v.49, no.1, 2006년, pp.55-60 
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( Caffeic Acid O-Methyltransferase from Populus deltoides: Functional Expression and Characterization ) |
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| 초 록 |
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| Enzymatic O-methylation, catalyzed by S-adenosyl-L-methionine (SAM)-dependent O-methyltranferases (OMTs), is a ubiquitous reaction, occurring in almost all living organisms. Plant OMTs are involved in the methylation of secondary metabolites, including phenylpropanoid and flavonoid compounds. Here, we used RT-PCR to isolate and characterize POMT-2 from Populus deltoides. This OMT comprises a 1095-b open reading frame that encodes a 39.7-kDa protein. BLAST results showed $87%$ identities to an OMT from Prunus dulcis and a caffeic acid OMT from Rosa chinensis. POMT-2 was expressed in Escherichia coli as a glutathione S-transferase fusion protein, and was purified by affinity chromatography. POMT-2 transferred a methyl group of SAM to caffeic acid and 6,7-dihydroxyflavone, but showed low activities toward quercetin and kaempferol. According to its in vitro substrate preference and composition of phenolic compounds in poplar, the in vivo function of POMT-2 is probably the methylation of caffeic acid and an involvement in lignin biosynthesis. |
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| 키워드 |
| caffeic acid;flavonoids;O-methyltransferase; |
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Journal of Plant Biology / v.49, no.1, 2006년, pp.55-60
한국식물학회
ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO200614222987341)
언어 : 영어 |
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| 논문 제공 : KISTI 한국과학기술정보연구원 |
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