Author
![]() |
Ralph, John |
![]() |
MARITA, JANE - USDFRC |
![]() |
LU, FACHUANG - UW MADISON |
![]() |
LAPIERRE, CATHERINE - INRA-GRIGNON,FRANCE |
![]() |
BOERJAN, WOUT - U. GENT, BELGIUM |
![]() |
VAN DOORSSELAERE, JAN - U. GENT, BELGIUM |
![]() |
PILATE, GILLES - INRA-ORLEANS, FRANCE |
![]() |
JOUANIN, LISE - INRA-VERSAILLES, FRANCE |
|
Submitted to: Meeting Abstract
Publication Type: Proceedings Publication Acceptance Date: 6/3/2001 Publication Date: N/A Citation: N/A Interpretive Summary: Technical Abstract: COMT is the enzyme responsible for methylating 5-hydroxyconiferyl aldehyde, on the way to producing syringyl units. It is deficient in recently examined transgenic poplars downregulated by two different methods, a brown-midrib maize mutant (bm3), and in F5H-upregulated arabidopsis. In each case, 5-hydroxyconiferyl alcohol incorporated intimately into the lignin. Benzodioxane (4-O-beta/5-O-alpha) structures are produced and can be characterized by their beautiful NMR correlations, by their survival through DFRC-degradation, and their partial survival through thioacidolysis. The level of detail revealed by these methods provides reliable proof that the novel 5-hydroxyconiferyl alcohol monomer cross-couples with syringyl and guaiacyl units into the growing lignin oligomer, and that normal monolignols then add to the new 5-hydroxyguaiacyl terminus producing benzo-dioxanes. The endwise polymerization is therefore elegantly revealed, and is evidence that 5-hydroxyconiferyl alcohol should be recognized as an authentic lignin monomer in these angiosperms. |
