Asset Details
Do you wish to reserve the book?
A peroxisomally localized acyl-activating enzyme is required for volatile benzenoid formation in aPetunia×hybridacv. ‘Mitchell Diploid’ flower
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
A peroxisomally localized acyl-activating enzyme is required for volatile benzenoid formation in aPetunia×hybridacv. ‘Mitchell Diploid’ flower
Do you wish to request the book?
A peroxisomally localized acyl-activating enzyme is required for volatile benzenoid formation in aPetunia×hybridacv. ‘Mitchell Diploid’ flower
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
A peroxisomally localized acyl-activating enzyme is required for volatile benzenoid formation in aPetunia×hybridacv. ‘Mitchell Diploid’ flower
2012
Overview
Floral volatile benzenoid/phenylpropanoid (FVBP) biosynthesis is a complex and coordinate cellular process executed by petal limb cells of aPetunia×hybridacv. ‘Mitchell Diploid’ (MD) plant. In MD flowers, the majority of benzenoid volatile compounds are derived from a core phenylpropanoid pathway intermediate by a coenzyme A (CoA) dependent, β-oxidative scheme. Metabolic flux analysis, reverse genetics, and biochemical characterizations of key enzymes in this pathway have supported this putative concept. However, the theoretical first enzymatic reaction, which leads to the production of cinnamoyl-CoA, has only been physically demonstrated in a select number of bacteria likeStreptomyces maritimusthrough mutagenesis and recombinant protein production. A transcript has been cloned and characterized from MD flowers that shares high homology with anArabidopsis thalianatranscriptACYL-ACTIVATING ENZYME11(AtAAE11) and theS. maritimus ACYL-COA:LIGASE(SmEncH). In MD, thePhAAEtranscript accumulates in a very similar manner as bona fide FVBP network genes, i.e. high levels in an open flower petal and ethylene regulated.In planta, PhAAE is localized to the peroxisome. Upon reduction ofPhAAEtranscript through a stable RNAi approach, transgenic flowers emitted a reduced level of all benzenoid volatile compounds. Together, the data suggest that PhAAE may be responsible for the activation oft-cinnamic acid, which would be required for floral volatile benzenoid production in MD.
