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  1. Journal of the Korean Society for Applied Biological Chemistry
  2. Journal of the Korean Society for Applied Biological Chemistry : Volume 52
  3. Journal of the Korean Society for Applied Biological Chemistry : Volume 52, Issue 2, April 2009
  4. O-Methyltransferase from Soybean Uses Both Caffeoyl-CoA and Flavonoids as Substrates
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Journal of the Korean Society for Applied Biological Chemistry : Volume 60
Journal of the Korean Society for Applied Biological Chemistry : Volume 59
Journal of the Korean Society for Applied Biological Chemistry : Volume 58
Journal of the Korean Society for Applied Biological Chemistry : Volume 57
Journal of the Korean Society for Applied Biological Chemistry : Volume 56
Journal of the Korean Society for Applied Biological Chemistry : Volume 55
Journal of the Korean Society for Applied Biological Chemistry : Volume 54
Journal of the Korean Society for Applied Biological Chemistry : Volume 53
Journal of the Korean Society for Applied Biological Chemistry : Volume 52
Journal of the Korean Society for Applied Biological Chemistry : Volume 52, Issue 6, December 2009
Journal of the Korean Society for Applied Biological Chemistry : Volume 52, Issue 5, October 2009
Journal of the Korean Society for Applied Biological Chemistry : Volume 52, Issue 4, August 2009
Journal of the Korean Society for Applied Biological Chemistry : Volume 52, Issue 3, June 2009
Journal of the Korean Society for Applied Biological Chemistry : Volume 52, Issue 2, April 2009
Kinetics of Recombinant β-Secretase and Its Application to Inhibitor Screening
O-Methyltransferase from Soybean Uses Both Caffeoyl-CoA and Flavonoids as Substrates
Identification of Differential Gene Expression in Juvenile vs. Mature Leaves of Pear (Pyrus pyrifolia) by Using Annealing Control Primer
Acyclic Diterpenoids from the Leaves of Capsicum annuum
Effect of Sophora japonica Extract on Lipid Content in High Fat Diet Fed Rats
Characterization of Isoflavones Accumulation in Developing Leaves of Soybean (Glycine max) Cultivars
Hairy Root Cultures of Taxus cuspidate for Enhanced Production of Paclitaxel
Effects of Light and Temperature on Antioxidant Activity and Peroxidase Expression at Different Growth Stages of the Chinese Red Radish
Effects of Aralia continentalis and Angelica biserrata on Inflammatory Response in Lipopolysaccharide-Induced RAW 264.7 Macrophages and Phorbol Ester-induced Ear Edema
Anticoagulant Properties of Alizarin and Its Derivatives Derived from the Seed Extract of Cassia obtusifolia
Induction of Apoptosis in SNU-16 Human Gastric Cancer Cells by the Chloroform Fraction of an Extract of Dangyuja (Citrus grandis Leaves
Evaluation of a Pyrethrum Emulsion Prepared in Food-acceptable Components in Controlling Green Peach Aphid (Myzus persciae)
Weight Gain Limitation and Liver Protection by Long-Term Feeding of Astaxanthin in Murines
Metabolic Fingerprinting Study on the Substantial Equivalence of Genetically Modified (GM) Chinese Cabbage to Non-GM Cabbage
The Effect of Black Tea on Biomarkers of Metabolic Syndrome in High Fat Diet Fed Rats
Change of Ginsenoside Composition of Various American Ginseng Roots
Antimicrobial Activities of 2-Methyl-8-Hydroxyquinoline and Its Derivatives against Human Intestinal Bacteria
Journal of the Korean Society for Applied Biological Chemistry : Volume 52, Issue 1, February 2009

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O-Methyltransferase from Soybean Uses Both Caffeoyl-CoA and Flavonoids as Substrates

Content Provider Springer Nature Link
Author Kim, Bong Gyu Park, Yong Bae Chong, Youhoon Ahn, Joong Hoon Min, Shin Young Lee, Jung Bok Lee, Yoon Jung Kim, Jong Chan Park, So Hyun Lim, Yoongho Kim, Na Yeon Kim, Dae Hwan
Copyright Year 2003
Abstract A gene encoding O-methyltransferase (SOMT)-10 from soybean, SOMT-10, was cloned by reverse transcription polymerase chain reaction. Phylogenetic analysis revealed that SOMT-10 belonged to caffeoyl-CoA O-methyltransferase (CCoAOMT) and contained conserved catalytic residues found in CCoAOMT. SOMT-10 was expressed in Escherichia coli as a glutathione S-transferase fusion protein and purified to determine its substrate. Several compounds including caffeoyl-CoA, naringenin, quercetin, caffeic acid, kaempferol and luteonin were tested as substrates for the purified recombinant SOMT-10. Analysis of reaction products using high performance liquid chromatography revealed that SOMT-10 used caffeoyl-CoA, quercetin and luteolin as substrates. This result indicated that SOMT-10 used flavones having vicinal hydroxyl groups. The methylation position was determined to be the 3′ hydroxyl group. It is likely that SOMT-10 is a new class of OMT that uses not only caffeoyl-CoA, but also flavonoids. Molecular docking of tricetin with the modeled structure SOMT-10 disclosed that SOMT-10 showed all combinations of the O-methylated products.
Starting Page 114
Ending Page 120
Page Count 7
File Format PDF
ISSN 17382203
Journal Journal of the Korean Society for Applied Biological Chemistry
Volume Number 52
Issue Number 2
e-ISSN 2234344X
Language English
Publisher Springer-Verlag
Publisher Date 2003-01-01
Publisher Place New York
Access Restriction Subscribed
Subject Keyword soybean O-methyltransferase Applied Microbiology Biological Techniques caffeoyl-CoA Flavonoid Bioorganic Chemistry Phenylpropanoid
Content Type Text
Resource Type Article
Subject Organic Chemistry Biochemistry, Genetics and Molecular Biology
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