Publications

• Understanding in vivo benzenoid metabolism in petunia petal tissue.

  Boatright J., Negre F., Chen X., Kish C.M., Wood B., Peel G., Orlova I., Gang D., Rhodes D., Dudareva N.

  In vivo stable isotope labeling and computer-assisted metabolic flux analysis were used to investigate the metabolic pathways in petunia (Petunia hybrida) cv Mitchell leading from Phe to benzenoid compounds, a process that requires the shortening of the side chain by a C(2) unit. Deuterium-labeled ... >> More

  In vivo stable isotope labeling and computer-assisted metabolic flux analysis were used to investigate the metabolic pathways in petunia (Petunia hybrida) cv Mitchell leading from Phe to benzenoid compounds, a process that requires the shortening of the side chain by a C(2) unit. Deuterium-labeled Phe ((2)H(5)-Phe) was supplied to excised petunia petals. The intracellular pools of benzenoid/phenylpropanoid-related compounds (intermediates and end products) as well as volatile end products within the floral bouquet were analyzed for pool sizes and labeling kinetics by gas chromatography-mass spectrometry and liquid chromatography-mass spectrometry. Modeling of the benzenoid network revealed that both the CoA-dependent, beta-oxidative and CoA-independent, non-beta-oxidative pathways contribute to the formation of benzenoid compounds in petunia flowers. The flux through the CoA-independent, non-beta-oxidative pathway with benzaldehyde as a key intermediate was estimated to be about 2 times higher than the flux through the CoA-dependent, beta-oxidative pathway. Modeling of (2)H(5)-Phe labeling data predicted that in addition to benzaldehyde, benzylbenzoate is an intermediate between l-Phe and benzoic acid. Benzylbenzoate is the result of benzoylation of benzyl alcohol, for which activity was detected in petunia petals. A cDNA encoding a benzoyl-CoA:benzyl alcohol/phenylethanol benzoyltransferase was isolated from petunia cv Mitchell using a functional genomic approach. Biochemical characterization of a purified recombinant benzoyl-CoA:benzyl alcohol/phenylethanol benzoyltransferase protein showed that it can produce benzylbenzoate and phenylethyl benzoate, both present in petunia corollas, with similar catalytic efficiencies. << Less

  Plant Physiol. 135:1993-2011(2004) [PubMed] [EuropePMC]

  This publication is cited by 13 other entries.

• Characterization of benzylalcohol acetyltransferases in scented and non-scented Clarkia species.

  Nam K.H., Dudareva N., Pichersky E.

  The floral scent of Clarkia breweri, an annual native to California, contains copious amounts of benzylacetate, which is synthesized by a reaction of benzylalcohol and acetyl-CoA that is catalyzed by acetyl-CoA:benzylalcohol acetyltransferase (BEAT). Here we demonstrate that different lines of C. ... >> More

  The floral scent of Clarkia breweri, an annual native to California, contains copious amounts of benzylacetate, which is synthesized by a reaction of benzylalcohol and acetyl-CoA that is catalyzed by acetyl-CoA:benzylalcohol acetyltransferase (BEAT). Here we demonstrate that different lines of C. breweri contain different levels of BEAT activity even though they have similar levels of BEAT mRNA. We also present evidence that the genome of C. breweri's non-scented progenitor, C. concinna, contains BEAT genes, but that its flowers have little BEAT enzymatic activity. This is due to the fact that although C. concinna BEAT genes are transcribed in the flowers, the single intron in these transcripts is almost never spliced out, and when the intron is spliced out, the resulting enzyme has higher affinity with substrates other than benzylalcohol. These results indicate that the regulation of BEAT activity in Clarkia involves post-transcriptional mechanisms. << Less

  Plant Cell Physiol. 40:916-923(1999) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• Acetyl-CoA:benzylalcohol acetyltransferase--an enzyme involved in floral scent production in Clarkia breweri.

  Dudareva N., D'Auria J.C., Nam K.H., Raguso R.A., Pichersky E.

  Volatile esters impart distinct characteristics to the floral scent of many plants, and are important in attracting insect pollinators. They are also important flavor compounds in fruits. The ester benzylacetate is a major constituent of the floral scent of Clarkia breweri, an annual plant native ... >> More

  Volatile esters impart distinct characteristics to the floral scent of many plants, and are important in attracting insect pollinators. They are also important flavor compounds in fruits. The ester benzylacetate is a major constituent of the floral scent of Clarkia breweri, an annual plant native to California. The enzyme acetyl-CoA:benzylalcohol acetyltransferase (BEAT), which catalyzes the formation of benzylacetate, has been purified from C. breweri petals, and a cDNA encoding this enzyme has been isolated and characterized. The sequence of the 433-residue BEAT protein does not show high similarity to any previously characterized protein, but a 35-residue region from position 135-163 has significant similarity (42-56% identity) to several proteins known or suspected to use an acyl-CoA substrate. E. coli cells expressing C. breweri BEAT produced enzymatically active protein, and also synthesized benzylacetate and secreted it into the medium. Of the different parts of the C. breweri flower, petals contained the majority of BEAT transcripts, and no BEAT mRNA was detected in leaves. The levels of BEAT mRNA in the petals increased as the bud matured, and peaked at anthesis, paralleling changes in BEAT activity. However, three days after anthesis, mRNA levels began a steep decline, whereas BEAT activity remained high for the next two days, suggesting that the BEAT protein is relatively stable. << Less

  Plant J. 14:297-304(1998) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.