A peroxisomally localized acyl-activating enzyme is required for volatile benzenoid formation in a Petuniaxhybrida cv. 'Mitchell Diploid' flower

Floral volatile benzenoid/phenylpropanoid (FVBP) biosynthesis is a complex and coordinate cellular process executed by petal limb cells of a Petunia×hybrida cv. 'Mitchell Diploid' (MD) plant. In MD flowers, the majority of benzenoid volatile compounds are derived from a core phenylpropanoi...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 63(2012), 13 vom: 30. Aug., Seite 4821-33
1. Verfasser: Colquhoun, Thomas A (VerfasserIn)
Weitere Verfasser: Marciniak, Danielle M, Wedde, Ashlyn E, Kim, Joo Young, Schwieterman, Michael L, Levin, Laura A, Van Moerkercke, Alex, Schuurink, Robert C, Clark, David G
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2012
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Benzene Derivatives DNA, Plant Plant Proteins Propanols RNA, Messenger RNA, Plant Recombinant Proteins mehr... 1-phenylpropanol 0F897O3O4M
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100 1 |a Colquhoun, Thomas A  |e verfasserin  |4 aut 
245 1 2 |a A peroxisomally localized acyl-activating enzyme is required for volatile benzenoid formation in a Petuniaxhybrida cv. 'Mitchell Diploid' flower 
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520 |a Floral volatile benzenoid/phenylpropanoid (FVBP) biosynthesis is a complex and coordinate cellular process executed by petal limb cells of a Petunia×hybrida cv. '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 like Streptomyces maritimus through mutagenesis and recombinant protein production. A transcript has been cloned and characterized from MD flowers that shares high homology with an Arabidopsis thaliana transcript ACYL-ACTIVATING ENZYME11 (AtAAE11) and the S. maritimus ACYL-COA:LIGASE (SmEncH). In MD, the PhAAE transcript 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 of PhAAE transcript 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 of t-cinnamic acid, which would be required for floral volatile benzenoid production in MD 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
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650 7 |a DNA, Plant  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Propanols  |2 NLM 
650 7 |a RNA, Messenger  |2 NLM 
650 7 |a RNA, Plant  |2 NLM 
650 7 |a Recombinant Proteins  |2 NLM 
650 7 |a 1-phenylpropanol  |2 NLM 
650 7 |a 0F897O3O4M  |2 NLM 
700 1 |a Marciniak, Danielle M  |e verfasserin  |4 aut 
700 1 |a Wedde, Ashlyn E  |e verfasserin  |4 aut 
700 1 |a Kim, Joo Young  |e verfasserin  |4 aut 
700 1 |a Schwieterman, Michael L  |e verfasserin  |4 aut 
700 1 |a Levin, Laura A  |e verfasserin  |4 aut 
700 1 |a Van Moerkercke, Alex  |e verfasserin  |4 aut 
700 1 |a Schuurink, Robert C  |e verfasserin  |4 aut 
700 1 |a Clark, David G  |e verfasserin  |4 aut 
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