Coniferyl aldehyde 5-hydroxylation and methylation direct syringyl lignin biosynthesis in angiosperms.

@article{Osakabe1999ConiferylA5,
  title={Coniferyl aldehyde 5-hydroxylation and methylation direct syringyl lignin biosynthesis in angiosperms.},
  author={Keishi Osakabe and Calvin C. G. Tsao and Lin-Sheng Li and Jacqueline L. Popko and Toshiaki Umezawa and Daniel T. Carraway and R H Smeltzer and Chandrashekhar Pralhad Joshi and Vincent L Chiang},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 16},
  pages={
          8955-60
        }
}
A central question in lignin biosynthesis is how guaiacyl intermediates are hydroxylated and methylated to the syringyl monolignol in angiosperms. To address this question, we cloned cDNAs encoding a cytochrome P450 monooxygenase (LsM88) and a caffeate O-methyltransferase (COMT) from sweetgum (Liquidambar styraciflua) xylem. Mass spectrometry-based functional analysis of LsM88 in yeast identified it as coniferyl aldehyde 5-hydroxylase (CAld5H). COMT expressed in Escherichia coli methylated 5… CONTINUE READING

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