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Plant and Cell Physiology Advance Access published online on May 3, 2005
Plant and Cell Physiology, doi:10.1093/pcp/pci120
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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 Cheng1 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.
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