Matches in UGent Biblio for { <https://biblio.ugent.be/publication/112641#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B130253.
- aggregation creator B130254.
- aggregation creator B130255.
- aggregation creator B130256.
- aggregation creator B130257.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "1999".
- aggregation format "application/pdf".
- aggregation hasFormat 112641.bibtex.
- aggregation hasFormat 112641.csv.
- aggregation hasFormat 112641.dc.
- aggregation hasFormat 112641.didl.
- aggregation hasFormat 112641.doc.
- aggregation hasFormat 112641.json.
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- aggregation hasFormat 112641.mods.
- aggregation hasFormat 112641.rdf.
- aggregation hasFormat 112641.ris.
- aggregation hasFormat 112641.txt.
- aggregation hasFormat 112641.xls.
- aggregation hasFormat 112641.yaml.
- aggregation isPartOf urn:issn:0021-9258.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Evolution of plant defense mechanisms: relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductase".
- aggregation 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.".
- aggregation authorList BK334409.
- aggregation endPage "7527".
- aggregation issue "11".
- aggregation startPage "7516".
- aggregation volume "274".
- aggregation aggregates 4169158.
- aggregation isDescribedBy 112641.
- aggregation similarTo jbc.274.11.7516.
- aggregation similarTo LU-112641.