Characterization of an Isoflavonoid-Specific Prenyltransferase from Lupinus albus

Description:

Article on the characterization of an isoflavonoid-specific prenyltransferase from Lupinus albus.

Creator(s):
Creation Date: May 2012
Partner(s):
UNT College of Arts and Sciences
Collection(s):
UNT Scholarly Works
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Total Uses: 10
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Creator (Author):
Shen, Guoan

Samuel Roberts Noble Foundation

Creator (Author):
Huhman, David

Samuel Roberts Noble Foundation

Creator (Author):
Lei, Zhentian

Samuel Roberts Noble Foundation

Creator (Author):
Snyder, John

Samuel Roberts Noble Foundation

Creator (Author):
Sumner, Lloyd W.

Samuel Roberts Noble Foundation

Creator (Author):
Dixon, R. A.

University of North Texas; Samuel Roberts Noble Foundation

Publisher Info:
Place of Publication: [Rockville, Maryland]
Date(s):
  • Creation: May 2012
Description:

Article on the characterization of an isoflavonoid-specific prenyltransferase from Lupinus albus.

Degree:
Department: Biological Sciences
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.

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

Physical Description:

11 p.

Language(s):
Subject(s):
Keyword(s): Lupinus albus | isoflavonoids | prenyltransferase
Source: Plant Physiology, 2012, Rockville: American Society of Plant Biologists, pp. 70-80
Partner:
UNT College of Arts and Sciences
Collection:
UNT Scholarly Works
Identifier:
  • DOI: 10.1104/pp.112.195271
  • ARK: ark:/67531/metadc282594
Resource Type: Article
Format: Text
Rights:
Access: Public
Citation:
Publication Title: Plant Physiology
Volume: 159
Issue: 1
Page Start: 70
Page End: 80
Peer Reviewed: Yes