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|a DE-627
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|e rakwb
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|a eng
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|a Kim, B G
|e verfasserin
|4 aut
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|a Characterization of an O-methyltransferase from soybean
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|c 2006
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 07.02.2007
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|a Date Revised 13.12.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a O-methyltransferases (OMTs) catalyze the transfer of a methyl group from S-adenosine-L-methionine to a hydroxyl group of an acceptor molecule to form methyl ether derivatives and can modify the basic backbone of a secondary metabolite. A new O-methyltransferase, SOMT-9, was cloned from Glycine max and found to encode a protein whose molecular weight is 27-kDa. SOMT-9 was expressed as a GST-fusion protein in Escherichia coli and several compounds such as caffeic acid, esculetin, narigenin, kaempferol, quercetin, and luteolin were tested as putative substrates of SOMT-9. HPLC and NMR results showed that SOMT-9 transfers a methyl group to the 3'-OH group of substrates having ortho-hydroxyl groups. SOMT-9 showed the highest affinity for quercetin, suggesting that SOMT-9 uses a flavonoid as a substrate. Based on its molecular weight and substrate specificity, SOMT-9 belongs to a new class of OMT and is likely to be involved in the biosynthesis of isorhamnetin
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Protein O-Methyltransferase
|2 NLM
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|a EC 2.1.1.-
|2 NLM
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|a Lee, H J
|e verfasserin
|4 aut
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|a Park, Y
|e verfasserin
|4 aut
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|a Lim, Y
|e verfasserin
|4 aut
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|a Ahn, J-H
|e verfasserin
|4 aut
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 44(2006), 4 vom: 15. Apr., Seite 236-41
|w (DE-627)NLM098178261
|x 0981-9428
|7 nnns
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| 773 |
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|g volume:44
|g year:2006
|g number:4
|g day:15
|g month:04
|g pages:236-41
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|d 44
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|h 236-41
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