Skip Navigation


Plant and Cell Physiology Advance Access first published online on May 3, 2005
This version published online on May 3, 2005
Plant and Cell Physiology, doi:10.1093/pcp/pci120
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
46/7/1073    most recent
pci120v2
pci120v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Li, L.
Right arrow Articles by Chiang, V. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Li, L.
Right arrow Articles by Chiang, V. L.
Agricola
Right arrow Articles by Li, L.
Right arrow Articles by Chiang, V. L.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology 2005 © The Japanese Society of Plant Physiologists (JSPP); all rights reserved.
Received February 12, 2005
Accepted April 27, 2005

Regular Paper

Clarification of Cinnamoyl Co-Enzyme a Reductase Catalysis in Monolignol Biosynthesis of Aspen

Laigeng Li 1*, Xiaofei Cheng 1, Shanfa Lu 1, Tomoyuki Nakatsubo 2, Toshiaki Umezawa 2, and Vincent L. Chiang 1

1 Forest Biotechnology Group, Department of Forestry, North Carolina State University, Raleigh, NC 27695-7247, USA
2 Laboratory of Metabolic Science of Forest Plants and Microorganisms, Research Institute for Sustainable Humanosphere, Kyoto University, Uji, Kyoto 611-0011, Japan

* To whom correspondence should be addressed.
Laigeng Li, E-mail: Laigeng_Li{at}ncsu.edu


  Abstract

Cinnamoyl Co-enzyme A reductase (CCR), one of the key enzymes involved in the biosynthesis of monolignols, has been thought to catalyze the conversion of several cinnamoyl CoA esters to their respective cinnamaldehydes. However, it is unclear which cinnamoyl CoA ester is metabolized for monolignol biosynthesis. A xylem-specific CCR cDNA was cloned from aspen (Populus tremuloides) developing xylem tissue. The recombinant CCR protein was produced through an E. coli expression system and purified to electrophoretic homogeneity. CCR biochemical properties were characterized through direct structural corroboration and quantitative analysis of the reaction products using a liquid chromatography-mass spectrometry system. The enzyme kinetics demonstrated that CCR selectively catalyzed the reduction of feruloyl-CoA from a mixture of five cinnamoyl CoA esters. Furthermore, feruloyl-CoA showed a strong competitive inhibition on the CCR catalysis of other cinnamoyl CoA esters. Importantly, when CCR was coupled with caffeoyl-CoA O-methyltransferase (CCoAOMT) to catalyze the substrate of caffeoyl-CoA ester, coniferaldehyde was formed, suggesting that CCoAOMT and CCR are neighboring enzymes. However, the in vitro results also revealed that the reactions mediated by these two neighboring enzymes require different pH environments, indicating that compartmentalization is likely needed for CCR and CCoAOMT to function properly in vivo. Eight CCR homologous genes were identified in P. trichocarpa genome and their expression profiling suggests that they may function differentially.

Keywords: Cinnamoyl Co-enzyme A reductase (CCR); monolignol biosynthesis; lignin; xylem.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Plant Physiol.Home page
R. D. Mellway, L. T. Tran, M. B. Prouse, M. M. Campbell, and C. P. Constabel
The Wound-, Pathogen-, and Ultraviolet B-Responsive MYB134 Gene Encodes an R2R3 MYB Transcription Factor That Regulates Proanthocyanidin Synthesis in Poplar
Plant Physiology, June 1, 2009; 150(2): 924 - 941.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
J.-C. Leple, R. Dauwe, K. Morreel, V. Storme, C. Lapierre, B. Pollet, A. Naumann, K.-Y. Kang, H. Kim, K. Ruel, et al.
Downregulation of Cinnamoyl-Coenzyme A Reductase in Poplar: Multiple-Level Phenotyping Reveals Effects on Cell Wall Polymer Metabolism and Structure
PLANT CELL, November 1, 2007; 19(11): 3669 - 3691.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
S. Lu, Y. Zhou, L. Li, and V. L. Chiang
Distinct Roles of Cinnamate 4-hydroxylase Genes in Populus
Plant Cell Physiol., July 1, 2006; 47(7): 905 - 914.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.