کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2016876 | 1067705 | 2006 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization of an O-methyltransferase from soybean
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موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
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 3â²-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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Plant Physiology and Biochemistry - Volume 44, Issue 4, April 2006, Pages 236-241
Journal: Plant Physiology and Biochemistry - Volume 44, Issue 4, April 2006, Pages 236-241
نویسندگان
B.G. Kim, H.J. Lee, Y. Park, Y. Lim, J.-H. Ahn,