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231223s2009 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2009.08.004
|2 doi
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|a pubmed25n0637.xml
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|a (DE-627)NLM191163961
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|a (NLM)19733090
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Kim, Dea Hwan
|e verfasserin
|4 aut
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| 245 |
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|a Molecular characterization of flavonoid malonyltransferase from Oryza sativa
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|c 2009
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 26.03.2010
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a In this study, a flavonoid malonyltransferase (OsMaT-2) was cloned from Oryza sativa, and the recombinant protein OsMaT-2 was purified via affinity chromatography. OsMaT-2 utilized a variety of flavonoid glucosides, including flavanone glucosides, flavone glucosides, flavonol glucosides, and isoflavone glucosides as substrates, but did not utilize anthocyanin. As an acyl donor, OsMaT-2 utilized only malonyl-CoA. Based on reactions with various quercetin 3-O-sugars, we identified the probable position of malonylation as the 6''-hydroxyl group of the sugar. This is the first report, to the best of our knowledge, of the cloning of a flavonoid malonyltransferase from O. sativa
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Carbohydrates
|2 NLM
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|a DNA, Complementary
|2 NLM
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|a DNA, Plant
|2 NLM
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|a Plant Proteins
|2 NLM
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|a RNA, Plant
|2 NLM
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|a Recombinant Proteins
|2 NLM
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|a Malonyl Coenzyme A
|2 NLM
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|a 524-14-1
|2 NLM
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|a Quercetin
|2 NLM
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|a 9IKM0I5T1E
|2 NLM
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|a Acyltransferases
|2 NLM
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|a EC 2.3.-
|2 NLM
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1 |
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|a Kim, Seong Kyong
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kim, Jeong-Ho
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kim, Bong-Gyu
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Ahn, Joong-Hoon
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 47(2009), 11-12 vom: 18. Nov., Seite 991-7
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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|g volume:47
|g year:2009
|g number:11-12
|g day:18
|g month:11
|g pages:991-7
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|u http://dx.doi.org/10.1016/j.plaphy.2009.08.004
|3 Volltext
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