Functional Characterization of Proanthocyanidin Pathway Enzymes from Tea and Their Application for Metabolic Engineering

Description:

Article on the functional characterization of proanthocyanidin pathway enzymes from tea and their application for metabolic engineering.

Creator(s):
Creation Date: March 2013
Partner(s):
UNT College of Arts and Sciences
Collection(s):
UNT Scholarly Works
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Total Uses: 8
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Creator (Author):
Pang, Yongzhen

Samuel Roberts Noble Foundation

Creator (Author):
Abeysinghe, I. Sarath B.

Tea Research Institute of Sri Lanka

Creator (Author):
He, Ji

Samuel Roberts Noble Foundation

Creator (Author):
He, Xian-Zhi

Samuel Roberts Noble Foundation

Creator (Author):
Huhman, David

Samuel Roberts Noble Foundation

Creator (Author):
Mewan, K. Mudith

Tea Research Institute of Sri Lanka

Creator (Author):
Sumner, Lloyd W.

Samuel Roberts Noble Foundation

Creator (Author):
Yun, Jianfei

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: March 2013
Description:

Article on the functional characterization of proanthocyanidin pathway enzymes from tea and their application for metabolic engineering.

Degree:
Department: Biological Sciences
Note:

Abstract: Tea (Camellia sinensis) is rich in specialized metabolites, especially polyphenolic proanthocyanidins (PAs) and their precursors. To better understand the PA pathway in tea, we generated a complementary DNA library from leaf tissue of the blister blight-resistant tea cultivar TRI2043 and functionally characterized key enzymes responsible for the biosynthesis of PA precursors. Structural genes encoding enzymes involved in the general phenylpropanoid/flavonoid pathway and the PA-specific branch pathway were well represented in the library. Recombinant tea leucoanthocyanidin reductase (CsLAR) expressed in Escherichia coli was active with leucocyanidin as substrate to produce the 2R,3S-trans-flavan-ol (+)-catechin in vitro. Two genes encoding anthocyanidin reductase, CsANR1 and CsANR2, were also expressed in E. coli, and the recombinant proteins exhibited similar kinetic properties. Both converted cyanidin to a mixture of (+)-epicatechin and (−)-catechin, although in different proportions, indicating that both enzymes possess epimerase activity. These epimers were unexpected based on the belief that tea PAs are made from (−)-epicatechin and (+)-catechin. Ectopic expression of CsANR2 or CsLAR led to the accumulation of low levels of PA precursors and their conjugates in Medicago truncatula hairy roots and anthocyanin-overproducing tobacco (Nicotiana tabacum), but levels of oligomeric PAs were very low. Surprisingly, the expression of CsLAR in tobacco overproducing anthocyanin led to the accumulation of higher levels of epicatechin and its glucoside than of catechin, again highlighting the potential importance of epimerization in flavan-3-ol biosynthesis. These data provide a resource for understanding tea PA biosynthesis and tools for the bioengineering of flavanols.

Note:

Copyright © 2013 American Society of Plant Biologists. The following article appeared in Plant Physiology, 161:3, pp. 1103-1116, http://www.plantphysiol.org/content/161/3/1103.long

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14 p.

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Subject(s):
Keyword(s): tea | Camellia sinensis | metabolites | polyphenolic proanthocyanidins
Source: Plant Physiology, 2013, Rockville: American Society of Plant Biologists, pp. 1103-1116
Partner:
UNT College of Arts and Sciences
Collection:
UNT Scholarly Works
Identifier:
  • DOI: 10.1104/pp.112.212050 |
  • ARK: ark:/67531/metadc282590
Resource Type: Article
Format: Text
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Access: Public
Citation:
Publication Title: Plant Physiology
Volume: 161
Issue: 3
Page Start: 1103
Page End: 1116
Peer Reviewed: Yes