Purification and characterization of peroxidases correlated with lignification in poplar xylem

  • Christensen J
  • Bauw G
  • Welinder K
 et al. 
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Lignin is an integral cell wall component of all vascular plants. Peroxidases are widely believed to catalyze the last enzymatic step in the biosynthesis of lignin, the dehydrogenation of the p-coumaryl alcohols. As the first stage in identifying lignin-specific peroxidase isoenzymes, the classical anionic peroxidases found in the xylem of poplar (Populus trichocarpa Trichobel) were purified and characterized. Five different poplar xylem peroxidases (PXP 1, PXP 2, PXP 3-4, PXP 5, and PXP 6) were isolated. All five peroxidases were strongly glycosylated (3.6% to 4.9% N-glucosamine), with apparent molecular masses between 46 and 54 kD and pI values between pH 3.1 and 3.8. Two of the five isolated peroxidases (PXP 3-4 and PXP 5) could oxidize the lignin monomer analog syringaldazine, an activity previously correlated with lignification in poplar. Because these isoenzymes were specifically or preferentially expressed in xylem, PXP 3-4 and PXP 5 are suggested to be involved in lignin polymerization.

Author-supplied keywords

  • Amino Acid
  • Amino Acid Sequence
  • Amino Acids/analysis
  • Glycosylation
  • Isoelectric Point
  • Isoenzymes/genetics/isolation & purification/metab
  • Lignin/*biosynthesis
  • Molecular Sequence Data
  • Molecular Weight
  • Non-U.S. Gov't
  • Peptide Fragments/genetics/isolation & purificatio
  • Peroxidases/genetics/*isolation & purification/met
  • Sequence Homology
  • Substrate Specificity
  • Support
  • Trees/*enzymology/genetics/metabolism

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  • J. H. Christensen

  • G. Bauw

  • K. G. Welinder

  • M. V. Montagu

  • W. Boerjan

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