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Evolution of plant defense mechanisms: relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductase

(1999) JOURNAL OF BIOLOGICAL CHEMISTRY. 274(11). p.7516-7527
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Abstract
Pinoresinol-lariciresinol and isoflavone reductase classes are phylogenetically related, as is a third, the so-called "isoflavone reductase homologs," This study establishes the first known catalytic function for the latter, as being able to engender the NADPH-dependent reduction of phenylcoumaran benzylic ethers, Accordingly, all three reductase classes are involved in the biosynthesis of important and related phenylpropanoid-derived plant defense compounds. In this investigation, the phenylcoumaran benzylic ether reductase from the gymnosperm, Pinus taeda, was cloned, with the recombinant protein heterologously expressed in Escherichia coli, The purified enzyme reduces the benzylic ether functionalities of both dehydrodiconiferyl alcohol and dihydrodehydrodiconiferyl alcohol, with a higher affinity for the former, as measured by apparent K-m and V-max values and observed kinetic H-3-isotope effects. It abstracts the 4R-hydride of the required NADPH cofactor in a manner analogous to that of the pinoresinol-lariciresinol reductases and isoflavone reductases. A similar catalytic function was observed for the corresponding recombinant reductase whose gene was cloned from the angiosperm, Populus trichocarpa. Interestingly, both pinoresinol-lariciresinol reductases and isoflavone reductases catalyze enantiospecific conversions, whereas the phenylcoumaran benzylic ether reductase only shows regiospecific discrimination. A possible evolutionary relationship among the three reductase classes is proposed, based on the supposition that phenylcoumaran benzylic ether reductases represent the progenitors of pinoresinol-lariciresinol and isoflavone reductases.
Keywords
CONIFER NEEDLES, CELL-DIVISION, STRESS RESPONSES, MOLECULAR-CLONING, PHENOLIC-COMPOUNDS, DILIGNOL GLYCOSIDES, FORSYTHIA-INTERMEDIA, PHYTOALEXIN BIOSYNTHESIS, MEDICAGO-SATIVA L, PIPER WIGHTII

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Citation

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Chicago
Gang, David R, Hiryuki Kasahara, Zhi-Qiang Xia, Kristine Vander Mijnsbrugge, Wout Boerjan, Marc Van Montagu, Laurence B Davin, and Norman G Lewis. 1999. “Evolution of Plant Defense Mechanisms: Relationships of Phenylcoumaran Benzylic Ether Reductases to Pinoresinol-lariciresinol and Isoflavone Reductase.” Journal of Biological Chemistry 274 (11): 7516–7527.
APA
Gang, D. R., Kasahara, H., Xia, Z.-Q., Vander Mijnsbrugge, K., Boerjan, W., Van Montagu, M., Davin, L. B., et al. (1999). Evolution of plant defense mechanisms: relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductase. JOURNAL OF BIOLOGICAL CHEMISTRY, 274(11), 7516–7527.
Vancouver
1.
Gang DR, Kasahara H, Xia Z-Q, Vander Mijnsbrugge K, Boerjan W, Van Montagu M, et al. Evolution of plant defense mechanisms: relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductase. JOURNAL OF BIOLOGICAL CHEMISTRY. 1999;274(11):7516–27.
MLA
Gang, David R, Hiryuki Kasahara, Zhi-Qiang Xia, et al. “Evolution of Plant Defense Mechanisms: Relationships of Phenylcoumaran Benzylic Ether Reductases to Pinoresinol-lariciresinol and Isoflavone Reductase.” JOURNAL OF BIOLOGICAL CHEMISTRY 274.11 (1999): 7516–7527. Print.
@article{112641,
  abstract     = {Pinoresinol-lariciresinol and isoflavone reductase classes are phylogenetically related, as is a third, the so-called {\textacutedbl}isoflavone reductase homologs,{\textacutedbl} This study establishes the first known catalytic function for the latter, as being able to engender the NADPH-dependent reduction of phenylcoumaran benzylic ethers, Accordingly, all three reductase classes are involved in the biosynthesis of important and related phenylpropanoid-derived plant defense compounds. In this investigation, the phenylcoumaran benzylic ether reductase from the gymnosperm, Pinus taeda, was cloned, with the recombinant protein heterologously expressed in Escherichia coli, The purified enzyme reduces the benzylic ether functionalities of both dehydrodiconiferyl alcohol and dihydrodehydrodiconiferyl alcohol, with a higher affinity for the former, as measured by apparent K-m and V-max values and observed kinetic H-3-isotope effects. It abstracts the 4R-hydride of the required NADPH cofactor in a manner analogous to that of the pinoresinol-lariciresinol reductases and isoflavone reductases. A similar catalytic function was observed for the corresponding recombinant reductase whose gene was cloned from the angiosperm, Populus trichocarpa. Interestingly, both pinoresinol-lariciresinol reductases and isoflavone reductases catalyze enantiospecific conversions, whereas the phenylcoumaran benzylic ether reductase only shows regiospecific discrimination. A possible evolutionary relationship among the three reductase classes is proposed, based on the supposition that phenylcoumaran benzylic ether reductases represent the progenitors of pinoresinol-lariciresinol and isoflavone reductases.},
  author       = {Gang, David R and Kasahara, Hiryuki and Xia, Zhi-Qiang and Vander Mijnsbrugge, Kristine and Boerjan, Wout and Van Montagu, Marc and Davin, Laurence B and Lewis, Norman G},
  issn         = {0021-9258},
  journal      = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  keyword      = {CONIFER NEEDLES,CELL-DIVISION,STRESS RESPONSES,MOLECULAR-CLONING,PHENOLIC-COMPOUNDS,DILIGNOL GLYCOSIDES,FORSYTHIA-INTERMEDIA,PHYTOALEXIN BIOSYNTHESIS,MEDICAGO-SATIVA L,PIPER WIGHTII},
  language     = {eng},
  number       = {11},
  pages        = {7516--7527},
  title        = {Evolution of plant defense mechanisms: relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductase},
  url          = {http://dx.doi.org/10.1074/jbc.274.11.7516},
  volume       = {274},
  year         = {1999},
}

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