%0 Journal Article %1 citeulike:892456 %A Zhao, Y. %A Christensen, S. K. %A Fankhauser, C. %A Cashman, J. R. %A Cohen, J. D. %A Weigel, D. %A Chory, J. %C Howard Hughes Medical Institute, Plant Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, CA 92037, USA. %D 2001 %J Science %K n-oxidation flavin oxygenases %N 5502 %P 306--309 %R 10.1126/science.291.5502.306 %T A role for flavin monooxygenase-like enzymes in auxin biosynthesis. %U http://dx.doi.org/10.1126/science.291.5502.306 %V 291 %X Although auxin is known to regulate many processes in plant development and has been studied for over a century, the mechanisms whereby plants produce it have remained elusive. Here we report the characterization of a dominant Arabidopsis mutant, yucca, which contains elevated levels of free auxin. YUCCA encodes a flavin monooxygenase-like enzyme and belongs to a family that includes at least nine other homologous Arabidopsis genes, a subset of which appears to have redundant functions. Results from tryptophan analog feeding experiments and biochemical assays indicate that YUCCA catalyzes hydroxylation of the amino group of tryptamine, a rate-limiting step in tryptophan-dependent auxin biosynthesis.

@article{citeulike:892456, abstract = {Although auxin is known to regulate many processes in plant development and has been studied for over a century, the mechanisms whereby plants produce it have remained elusive. Here we report the characterization of a dominant Arabidopsis mutant, yucca, which contains elevated levels of free auxin. YUCCA encodes a flavin monooxygenase-like enzyme and belongs to a family that includes at least nine other homologous Arabidopsis genes, a subset of which appears to have redundant functions. Results from tryptophan analog feeding experiments and biochemical assays indicate that YUCCA catalyzes hydroxylation of the amino group of tryptamine, a rate-limiting step in tryptophan-dependent auxin biosynthesis.}, added-at = {2006-10-23T11:08:30.000+0200}, address = {Howard Hughes Medical Institute, Plant Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, CA 92037, USA.}, author = {Zhao, Y. and Christensen, S. K. and Fankhauser, C. and Cashman, J. R. and Cohen, J. D. and Weigel, D. and Chory, J.}, biburl = {https://www.bibsonomy.org/bibtex/294c3c774bca109916608a64df82b0a7d/robert}, citeulike-article-id = {892456}, doi = {10.1126/science.291.5502.306}, interhash = {68d7511c168dbcbe068f0fcd4f4e8de0}, intrahash = {94c3c774bca109916608a64df82b0a7d}, issn = {0036-8075}, journal = {Science}, keywords = {n-oxidation flavin oxygenases}, month = {January}, number = 5502, pages = {306--309}, priority = {2}, timestamp = {2006-10-23T11:08:30.000+0200}, title = {A role for flavin monooxygenase-like enzymes in auxin biosynthesis.}, url = {http://dx.doi.org/10.1126/science.291.5502.306}, volume = 291, year = 2001 }