Characterization of an Isoflavonoid-Specific Prenyltransferase from Lupinus albus Metadata
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- Main Title Characterization of an Isoflavonoid-Specific Prenyltransferase from Lupinus albus
Author: Shen, GuoanCreator Type: PersonalCreator Info: Samuel Roberts Noble Foundation
Author: Huhman, DavidCreator Type: PersonalCreator Info: Samuel Roberts Noble Foundation
Author: Lei, ZhentianCreator Type: PersonalCreator Info: Samuel Roberts Noble Foundation
Author: Snyder, JohnCreator Type: PersonalCreator Info: Samuel Roberts Noble Foundation
Author: Sumner, Lloyd W.Creator Type: PersonalCreator Info: Samuel Roberts Noble Foundation
Author: Dixon, R. A.Creator Type: PersonalCreator Info: University of North Texas; Samuel Roberts Noble Foundation
Name: Association Society of Plant BiologistsPlace of Publication: [Rockville, Maryland]
- Creation: 2012-05
- Content Description: Article on the characterization of an isoflavonoid-specific prenyltransferase from Lupinus albus.
- Physical Description: 11 p.
- Keyword: Lupinus albus
- Keyword: isoflavonoids
- Keyword: prenyltransferase
- Journal: Plant Physiology, 2012, Rockville: American Society of Plant Biologists, pp. 70-80
- Publication Title: Plant Physiology
- Volume: 159
- Issue: 1
- Page Start: 70
- Page End: 80
- Peer Reviewed: True
Name: UNT Scholarly WorksCode: UNTSW
Name: UNT College of Arts and SciencesCode: UNTCAS
- Rights Access: public
- DOI: 10.1104/pp.112.195271
- Archival Resource Key: ark:/67531/metadc282594
- Academic Department: Biological Sciences
- Display Note: Abstract: Prenylated flavonoids and isoflavonoids possess antimicrobial activity against fungal pathogens of plants. However, only a few plant flavonoid and isoflavonoid prenyltransferase genes have been identified to date. In this study, an isoflavonoid prenyltransferase gene, designated as LaPT1, was identified from white lupin (Lupinus albus). The deduced protein sequence of LaPT1 shared high homologies with known flavonoid and isoflavonoid prenyltransferases. The LaPT1 gene was mainly expressed in roots, a major site for constitutive accumulation of prenylated isoflavones in white lupin. LaPT1 is predicted to be a membrane-bound protein with nine transmembrane regions and conserved functional domains similar to other flavonoid and isoflavonoid prenyltransferases; it has a predicted chloroplast transit peptide and is plastid localized. A microsomal fraction containing recombinant LaPT1 prenylated the isoflavone genistein at the B-ring 3′ position to produce isowighteone. The enzyme is also active with 2′-hydroxygenistein but has no activity with other flavonoid substrates. The apparent Km of recombinant LaPT1 for the dimethylallyl diphosphate prenyl donor is in a similar range to that of other flavonoid prenyltransferases, but the apparent catalytic efficiency with genistein is considerably higher. Removal of the transit peptide increased the apparent overall activity but also increased the Km. Medicago truncatula hairy roots expressing LaPT1 accumulated isowighteone, a compound that is not naturally produced in this species, indicating a strategy for metabolic engineering of novel antimicrobial compounds in legumes.
- Display Note: Copyright © 2012 American Society of Plant Biologists. The following article appeared in Plant Physiology, 159:1, pp. 70-80, http://www.plantphysiol.org/content/159/1/70.long