title: 5-hydroxyconiferyl aldehyde modulates enzymatic methylation for syringyl monolignol formation, a new view of monolignol biosynthesis in angiosperms.
abstract: S-Adenosyl-L-methionine-dependent caffeate O-methyltransferase (COMT, EC 2.1.1.6) has traditionally been thought to catalyze the methylation of caffeate and 5- hydroxyferulate for the biosynthesis of syringyl monolignol, a lignin constituent of angiosperm wood that enables efficient lignin degradation for cellulose production. However, recent recognition that coniferyl aldehyde prevents 5-hydroxyferulate biosynthesis in lignifying tissue, and that the hydroxylated form of coniferyl aldehyde, 5-hydroxyconiferyl aldehyde, is an alternative COMT substrate, demands a re-evaluation of the role of COMT during monolignol biosynthesis. Based on recombinant aspen (Populus tremuloides) COMT enzyme kinetics coupled with mass spectrometry analysis, this study establishes for the first time that COMT is in fact a 5-hydroxyconiferyl aldehyde O-methyltransferase (AldOMT), and that 5-hydroxyconiferyl aldehyde is both the preferred AldOMT substrate and an inhibitor of caffeate and 5-hydroxyferulate methylation, as measured by K(m) and K(i) values. 5-Hydroxyconiferyl aldehyde also inhibited the caffeate and 5-hydroxyferulate methylation activities of xylem proteins from various angiosperm tree species. The evidence that syringyl monolignol biosynthesis is independent of caffeate and 5-hydroxyferulate methylation supports our previous discovery that coniferyl aldehyde prevents ferulate 5-hydroxylation and at the same time ensures a coniferyl aldehyde 5-hydroxylase (CAld5H)-mediated biosynthesis of 5-hydroxyconiferyl aldehyde. Together, our results provide conclusive evidence for the presence of a CAld5H/AldOMT-catalyzed coniferyl aldehyde 5-hydroxylation/methylation pathway that directs syringyl monolignol biosynthesis in angiosperms.
authors.affiliation: Plant Biotechnology Research Center, School of Forestry and Wood Products, Michigan Technological University, Houghton, Michigan 49931, USA.
authors.forename: L
authors.initials: L
authors.lastname: Li
authors.forename: J L
authors.initials: JL
authors.lastname: Popko
authors.forename: T
authors.initials: T
authors.lastname: Umezawa
authors.forename: V L
authors.initials: VL
authors.lastname: Chiang
mesh_terms: D000171:Acrolein / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D000447:Aldehydes / Q000494:pharmacology*; D002396:Catechols / Q000378:metabolism* / Q000494:pharmacology; D003373:Coumaric Acids / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004926:Escherichia coli; D006900:Hydroxylation; D007700:Kinetics; D008031:Lignin / Q000096:biosynthesis*; D019684:Magnoliopsida / Q000201:enzymology / Q000378:metabolism*; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism*; D008861:Microsomes / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000378:metabolism; D015394:Molecular Structure; D010940:Plant Proteins; D011994:Recombinant Proteins / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: C405696:5-hydroxyconiferyl aldehyde; D000447:Aldehydes; D002396:Catechols; D003373:Coumaric Acids; D004791:Enzyme Inhibitors; D010940:Plant Proteins; D011994:Recombinant Proteins; C071744:5-hydroxyferulic acid; D000171:Acrolein; D008031:Lignin; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; C120927:Ald5H protein, Liquidambar styraciflua; D008780:Methyltransferases; C019608:caffeate O-methyltransferase