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coniferaldehyde/pinus
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5 risultati
Purification, Characterization, and Cloning of Cinnamyl Alcohol Dehydrogenase in Loblolly Pine (Pinus taeda L.).
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Cinnamyl alcohol dehydrogenase (CAD, EC 1.1.1. 195) has been purified to homogeneity from differentiating xylem tissue and developing seeds of loblolly pine (Pinus taeda L.). The enzyme is a dimer with a native molecular weight of 82,000 and a subunit molecular weight of 44,000, and is the only form
Lignin structure in a mutant pine deficient in cinnamyl alcohol dehydrogenase.
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Cinnamyl alcohol dehydrogenase (CAD) activity is deficient in loblolly pine (Pinus taeda L.) harboring a mutated allele of the cad gene (cad-n1). We compared lignin structure of CAD-deficient and wild-type pines, both types segregating within full-sib families obtained by controlled crosses. The
Inheritance, gene expression, and lignin characterization in a mutant pine deficient in cinnamyl alcohol dehydrogenase.
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We have discovered a mutant loblolly pine (Pinus taeda L.) in which expression of the gene encoding cinnamyl alcohol dehydrogenase (CAD; EC 1.1.1.195) is severely reduced. The products of CAD, cinnamyl alcohols, are the precursors of lignin, a major cell wall polymer of plant vascular tissues.
Coniferyl alcohol metabolism in conifers -- II. Coniferyl alcohol and dihydroconiferyl alcohol biosynthesis.
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Coniferaldehyde and NADPH when incubated with microsomes isolated from developing xylem of Pinus strobus yielded coniferyl alcohol and dihydroconiferyl alcohol in vitro. D-(+)-Pinitol was also found to be a microsomal constituent. Endogenous E-coniferyl alcohol content, quantified in dormant buds,
Abnormal lignin in a loblolly pine mutant.
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Novel lignin is formed in a mutant loblolly pine (Pinus taeda L.) severely depleted in cinnamyl alcohol dehydrogenase (E.C. 1.1.1.195), which converts coniferaldehyde to coniferyl alcohol, the primary lignin precursor in pines. Dihydroconiferyl alcohol, a monomer not normally associated with the
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