PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32289635-1 2020 Caffeate 3-O-methyltransferase (COMT) catalyzes the methylation of the 3-hydroxyl group of caffeate to produce ferulate, an important precursor of the lignin biosynthesis. Lignin 151-157 caffeic acid 3-O-methyltransferase Zea mays 0-30 32289635-1 2020 Caffeate 3-O-methyltransferase (COMT) catalyzes the methylation of the 3-hydroxyl group of caffeate to produce ferulate, an important precursor of the lignin biosynthesis. Lignin 151-157 caffeic acid 3-O-methyltransferase Zea mays 32-36 32289635-3 2020 We hypothesized that a controlled inhibition of maize COMT can be an efficient approach to reduce ferulate and lignin, thus improving the saccharification process. Lignin 111-117 caffeic acid 3-O-methyltransferase Zea mays 54-58 30133138-1 2019 Caffeic acid O-methyltransferase (COMT), the lignin biosynthesis gene modified in many brown-midrib high-digestibility mutants of maize and sorghum, was targeted for downregulation in the small grain temperate cereal, barley (Hordeum vulgare), to improve straw properties. Lignin 45-51 caffeic acid 3-O-methyltransferase Zea mays 0-32 30133138-1 2019 Caffeic acid O-methyltransferase (COMT), the lignin biosynthesis gene modified in many brown-midrib high-digestibility mutants of maize and sorghum, was targeted for downregulation in the small grain temperate cereal, barley (Hordeum vulgare), to improve straw properties. Lignin 45-51 caffeic acid 3-O-methyltransferase Zea mays 34-38 29860438-4 2018 Moreover, competitive inhibition of the maize caffeoyl CoA O-methyltransferase (CCoAOMT) and caffeic acid O-methyltransferase (COMT) enzyme activities by SAH was found, suggesting that the SAH/SAM ratio, rather than the concentration of SAM, regulates the transmethylation reactions of lignin intermediates. Lignin 286-292 caffeic acid 3-O-methyltransferase Zea mays 93-125 29860438-4 2018 Moreover, competitive inhibition of the maize caffeoyl CoA O-methyltransferase (CCoAOMT) and caffeic acid O-methyltransferase (COMT) enzyme activities by SAH was found, suggesting that the SAH/SAM ratio, rather than the concentration of SAM, regulates the transmethylation reactions of lignin intermediates. Lignin 286-292 caffeic acid 3-O-methyltransferase Zea mays 127-131 29860438-6 2018 A remarkable increase in the unusual catechyl lignin in the mutant demonstrates that MTHFR down-regulation mainly affects guaiacyl lignin biosynthesis, consistent with the observation that CCoAOMT is more sensitive to SAH inhibition than COMT. Lignin 46-52 caffeic acid 3-O-methyltransferase Zea mays 238-242 20152036-1 2010 BACKGROUND: OMT (O-methyltransferase) genes are involved in lignin biosynthesis, which relates to stover cell wall digestibility. Lignin 60-66 caffeic acid 3-O-methyltransferase Zea mays 17-36 28594846-8 2017 Our genetic and biochemical data point toward a general mechanism whereby COMT is involved in the synthesis of both tricin and S lignin units. Lignin 129-135 caffeic acid 3-O-methyltransferase Zea mays 74-78 28013276-1 2017 Caffeoyl coenzyme A 3-O-methyltransferase (CCoAOMT) and caffeic acid-O-methyltransferase (COMT) are key enzymes in the biosynthesis of coniferyl and sinapyl alcohols, the precursors of guaiacyl (G) and syringyl (S) lignin subunits. Lignin 215-221 caffeic acid 3-O-methyltransferase Zea mays 56-88 28013276-1 2017 Caffeoyl coenzyme A 3-O-methyltransferase (CCoAOMT) and caffeic acid-O-methyltransferase (COMT) are key enzymes in the biosynthesis of coniferyl and sinapyl alcohols, the precursors of guaiacyl (G) and syringyl (S) lignin subunits. Lignin 215-221 caffeic acid 3-O-methyltransferase Zea mays 90-94 28013276-7 2017 On the other hand, the ccoaomt1 comt mutant displays phenotypic and lignin alterations similar to those already described for the comt mutant. Lignin 68-74 caffeic acid 3-O-methyltransferase Zea mays 32-36 28013276-9 2017 This suggests that the positive effect of lignin reduction on cell wall degradability of comt and ccoaomt1 comt mutants is counteracted by changes occurring in lignin composition, such as the decreased S/G ratio. Lignin 42-48 caffeic acid 3-O-methyltransferase Zea mays 89-93 28013276-9 2017 This suggests that the positive effect of lignin reduction on cell wall degradability of comt and ccoaomt1 comt mutants is counteracted by changes occurring in lignin composition, such as the decreased S/G ratio. Lignin 42-48 caffeic acid 3-O-methyltransferase Zea mays 107-111 28013276-9 2017 This suggests that the positive effect of lignin reduction on cell wall degradability of comt and ccoaomt1 comt mutants is counteracted by changes occurring in lignin composition, such as the decreased S/G ratio. Lignin 160-166 caffeic acid 3-O-methyltransferase Zea mays 89-93 28013276-9 2017 This suggests that the positive effect of lignin reduction on cell wall degradability of comt and ccoaomt1 comt mutants is counteracted by changes occurring in lignin composition, such as the decreased S/G ratio. Lignin 160-166 caffeic acid 3-O-methyltransferase Zea mays 107-111 23811284-7 2013 Consistent with the down regulation of COMT, the concentrations of p-coumaric acid, syringaldehydes, and lignin are reduced in P1-wr; Ufo1-1 internodes. Lignin 105-111 caffeic acid 3-O-methyltransferase Zea mays 39-43 23811284-18 2013 We show that lignin was reduced in Ufo1-1 plants expressing p1 and was associated with the post-transcriptional down regulation of CoA O-methyltransferase (COMT) enzyme. Lignin 13-19 caffeic acid 3-O-methyltransferase Zea mays 131-154 23811284-18 2013 We show that lignin was reduced in Ufo1-1 plants expressing p1 and was associated with the post-transcriptional down regulation of CoA O-methyltransferase (COMT) enzyme. Lignin 13-19 caffeic acid 3-O-methyltransferase Zea mays 156-160 18582385-3 2008 The greatest lignin reduction and the highest cell wall digestibility were observed in the brown-midrib-3 (bm3) mutant, which is disrupted in the caffeic acid O-methyltransferase (COMT) gene. Lignin 13-19 caffeic acid 3-O-methyltransferase Zea mays 91-105 18582385-3 2008 The greatest lignin reduction and the highest cell wall digestibility were observed in the brown-midrib-3 (bm3) mutant, which is disrupted in the caffeic acid O-methyltransferase (COMT) gene. Lignin 13-19 caffeic acid 3-O-methyltransferase Zea mays 146-178 18582385-3 2008 The greatest lignin reduction and the highest cell wall digestibility were observed in the brown-midrib-3 (bm3) mutant, which is disrupted in the caffeic acid O-methyltransferase (COMT) gene. Lignin 13-19 caffeic acid 3-O-methyltransferase Zea mays 180-184 18582385-9 2008 COMT disruption or down-regulation led to differential expressions of a few lignin pathway genes, which were all over-expressed, except for a phenylalanine ammonia-lyase gene. Lignin 76-82 caffeic acid 3-O-methyltransferase Zea mays 0-4 16941210-1 2006 The maize (Zea mays L.) caffeic acid O-methyl-transferase (COMT) is a key enzyme in the biosynthesis of lignin. Lignin 104-110 caffeic acid 3-O-methyltransferase Zea mays 24-57 16941210-1 2006 The maize (Zea mays L.) caffeic acid O-methyl-transferase (COMT) is a key enzyme in the biosynthesis of lignin. Lignin 104-110 caffeic acid 3-O-methyltransferase Zea mays 59-63 15536523-0 2004 Genetic diversity associated with variation in silage corn digestibility for three O-methyltransferase genes involved in lignin biosynthesis. Lignin 121-127 caffeic acid 3-O-methyltransferase Zea mays 83-102 12481050-5 2002 Biochemical analysis of COMT-AS showed: (a) a strong decrease in Klason lignin content at the flowering stage, (b) a decrease in syringyl units, (c) a lower p-coumaric acid content, and (d) the occurrence of unusual 5-OH guaiacyl units. Lignin 72-78 caffeic acid 3-O-methyltransferase Zea mays 24-28 7773015-4 1995 Here, we show that two independent brown midrib3 (bm3) mutations have resulted from structural changes in the COMT gene, which encodes the enzyme O-methyltransferase (COMT; EC 2.1.1.6), involved in lignin biosynthesis. Lignin 198-204 caffeic acid 3-O-methyltransferase Zea mays 110-114 7773015-4 1995 Here, we show that two independent brown midrib3 (bm3) mutations have resulted from structural changes in the COMT gene, which encodes the enzyme O-methyltransferase (COMT; EC 2.1.1.6), involved in lignin biosynthesis. Lignin 198-204 caffeic acid 3-O-methyltransferase Zea mays 167-171