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Lignins are cell wall phenolic heteropolymers which result from the oxidative coupling of three monolignols, p-coumaryl, coniferyl and sinapyl alcohol, in a reaction mediated by peroxidases. The most distinctive variation in the monomer composition of lignins in vascular plants is that found between the two main groups of seed plants. Thus, while gymnosperms lignins are typically composed of G units, with a minor proportion of H units, angiosperms lignins are largely composed of similar levels of G and S units. The presence of S units in angiosperm lignins raises certain concerns in relation with the step of lignin assembly due to the inability of most peroxidases to oxidize syringyl moieties. Zinnia elegans is currently used as a model for lignification studies: - first because of the simplicity and duality of the lignification pattern shown by hypocotyls and stems, in which hypocotyl lignins are typical of angiosperms, while young stem lignins partially resemble those occurring in gymnosperms. Secondly, because of the nature of the peroxidase isoenzyme complement, which is almost completely restricted to the presence of a basic peroxidase isoenzyme, which is capable of oxidizing both coniferyl and sinapyl alcohol, as well as both coniferyl and sinapyl aldehyde. In fact, the versatility of this enzyme is such that the substrate preference covers the three p-hydroxybenzaldehydes and the three p-hydroxycinnamic acids. The basic pI nature of this peroxidase is not an exceptional frame point in this system since basic peroxidases are differentially expressed during lignification in other model systems, show unusual and unique biochemical properties as regards the oxidation of syringyl moieties, and their down-regulation in transgenic plants leads to a reduction in lignin (G+S) levels. Basic peroxidase isoenzymes capable of oxidizing syringyl moieties are already present in basal gymnosperms, an observation that supports the idea that these enzymes were probably present in an ancestral plant species, pre-dating the early radiation of seed plants. It also suggests that the evolutionary gain of the monolignol branch which leads to the biosynthesis of sinapyl alcohol, and of course to syringyl lignins, was not only possible but also favored because the enzymes responsible for its polymerization had evolved previously. In this scenario, it is not surprising that these enzymes responsible for lignin construction appeared early in the evolution of land plants, and have been largely conserved during plant evolution.Abreviations: 4CL -p-hydroxycinnamate CoA ligase; C3H -p-coumarate-3-hydroxylase; C4H - cinnamate-4-hydroxylase; p-CA -p-coumaric acid; CAD - coniferyl alcohol dehydrogenase; CAld5H - coniferylaldehyde-5-hydroxylase; CCR -p-hydroxycinnamoyl-CoA reductase; CoI - compound I; CoII - compound II; G - guaiacyl unit; H -p-hydroxyphenyl unit; PAL - phenylalanine ammonia-lyase; S - syringyl unit.