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Functional characterization of caffeic acid

Fengyan WU, Zhenying WU, Aiguo YANG, Shanshan JIANG, Zeng-Yu WANG, Chunxiang FU

Frontiers of Agricultural Science and Engineering 2018, Volume 5, Issue 1, Pages 98-107 doi: 10.15302/J-FASE-2017198

Abstract: Caffeic acid -methyltransferase (COMT) is a crucial enzyme that mainly methylates phenylpropanoid -hydroxyl of C in the biosynthesis of syringyl lignin in angiosperms. A putative , named as , was isolated from switchgrass ( ), a C warm-season dual-purpose forage and bioenergy crop. Our results showed that recombinant PvCOMT1 enzyme protein catalyzed the methylation of 5-OH coniferyl alcohol, 5-OH coniferaldehyde (CAld5H) and 5-OH ferulic acid. Further studies indicate that CAld5H can dominate COMT-mediated reactions by inhibiting the methylation of the other substrates. Transgenic switchgrass plants generated by an RNAi approach were further employed to study the function of in internode lignification. A dramatic decrease in syringyl lignin units coupled with an obvious incorporation in 5-OH guaiacyl lignin units were observed in the COMT-RNAi transgenic plants. However, the constitutive suppression of COMT in switchgrass plants altered neither the pattern of lignin deposition along the stem nor the anatomical structure of internodes. Consistent with the biochemical characterization of PvCOMT1, a significant decrease in sinapaldehyde was found in the COMT-RNAi transgenic switchgrass plants, suggesting that CAld5H could be the optimal intermediate in the biosynthesis syringyl lignin.

Keywords： biofuel crop caffeic acid O-methyltransferase forage lignin Panicum virgatum switchgrass