Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Biochemical Characterization of the Suberization-Associated Anionic Peroxidase of Potato1

Mark A. Bernards2, *, Warren D. Fleming3, David B. Llewellyn4, Ronny Priefer4, Xiaolong Yang2, Anita Sabatino, and Guy L. Plourde

Program in Chemistry, University of Northern British Columbia, 3333 University Way, Prince George, British Columbia, Canada V2N 4Z9

The anionic peroxidase associated with the suberization response in potato (Solanum tuberosum L.) tubers during wound healing has been purified and partially characterized at the biochemical level. It is a 45-kD, class III (plant secretory) peroxidase that is localized to suberizing tissues and shows a preference for feruloyl (o-methoxyphenol)-substituted substrates (order of substrate preference: feruloyl > caffeoyl > p-coumaryl approx  syringyl) such as those that accumulate in tubers during wound healing. There was little influence on oxidation by side chain derivatization, although hydroxycinnamates were preferred over the corresponding hydroxycinnamyl alcohols. The substrate specificity pattern is consistent with the natural substrate incorporation into potato wound suberin. In contrast, the cationic peroxidase(s) induced in response to wound healing in potato tubers is present in both suberizing and nonsuberizing tissues and does not discriminate between hydroxycinnamates and hydroxycinnamyl alcohols. A synthetic polymer prepared using E-[8-13C]ferulic acid, H2O2, and the purified anionic enzyme contained a significant amount of cross-linking through C-8, albeit with retention of unsaturation.


1   This research was supported by a Natural Sciences and Engineering Research Council of Canada (NSERC) operating grant to M.A.B. D.B.L. was supported in part by a NSERC undergraduate scholarship.
2   Present address: Department of Plant Sciences, University of Western Ontario, London, ON, Canada N6A 5B7.
3   Present address: Department of Biology, University of Alberta, Edmonton, AB, Canada T6G 2E9.
4   Present address: Department of Chemistry, McGill University, Montreal, PQ, Canada H3A 1B1.
*   Corresponding author; e-mail bernards{at}julian.uwo.ca; fax 519-661-3935.

Plant Physiol. (1999) 121: 135-146
Copyright Clearance Center:   0032-0889/99/121//12
© 1999 American Society of Plant Physiologists




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