التفاصيل البيبلوغرافية
| العنوان: |
Functional reclassification of the putative cinnamyl alcohol dehydrogenase multigene family in Arabidopsis. |
| المؤلفون: |
Kim, Sung-Jin, Kim, Mi-Ran, Bedgar, Diana L., Moinuddin, Syed G. A., Cardenas, Claudia L., Davin, Laurence B., Chuthee Kang, Laurence B., Lewis, Norman G. |
| المصدر: |
Proceedings of the National Academy of Sciences of the United States of America; 2/10/2004, Vol. 101 Issue 6, p1455-1460, 6p |
| مصطلحات موضوعية: |
ALCOHOL dehydrogenase, GENES, ARABIDOPSIS, BRASSICACEAE, ALDEHYDES, ANGIOSPERMS |
| مستخلص: |
Of 17 genes annotated in the Arabidopsis genome database as cinnamyl alcohol dehydrogenase (CAD) homologues, an in silico analysis revealed that 8 genes were misannotated. Of the remaining nine, six were catalytically competent for NADPH-dependent reduction of p-coumaryl, caffeyl, coniferyl, 5-hydroxyconiferyl. and sinapyl aldehydes, whereas three displayed very low activity and only at very high substrate concentrations. Of the nine putative CADs, two (AtCAD5 and AtCAD4) had the highest activity and homology (≈83% similarity) relative to bona fide CADs from other species. AtCAD5 used all five substrates effectively, whereas AtCAD4 (of lower overall catalytic capacity) poorly used sinapyl aldehyde; the corresponding 270-fold decrease in k.nz resulted from higher Km and lower Kcat values, respectively. No CAD homologue displayed a specific requirement for sinapyl aldehyde, which was in direct contrast with unfounded claims for a so-called sinapyl alcohol dehydrogenase in angiosperms. AtCAD2, 3, as well as AtCAD7 and 8 (highest homology to sinapyl alcohol dehydrogenase) were catalytically less active over-all by at least an order of magnitude, due to increased Km and lower kcat values. Accordingly, alternative and/or bifunctional metabolic roles of these proteins in plant defense cannot be ruled out. Comprehensive analyses of lignified tissues of various Arabidopsis knockout mutants (for AtCAD5, 6, and 9) at different stages of growth/ development indicated the presence of functionally redundant CAD metabolic networks. Moreover, disruption of AtCADS expression had only a small effect on either overall lignin amounts deposited, or on syringyl-guaiacyl compositions, despite being the most catalytically active form in vitro. [ABSTRACT FROM AUTHOR] |
|
Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) |
| قاعدة البيانات: |
Complementary Index |
Full Text Finder