@article {Gang:2002p8027,
	title = {Characterization of phenylpropene O-methyltransferases from sweet basil: facile change of substrate specificity and convergent evolution within a plant O-methyltransferase family},
	journal = {Plant Cell},
	volume = {14},
	number = {2},
	year = {2002},
	month = {Feb},
	pages = {505{\textendash}19},
	abstract = {Some basil varieties are able to convert the phenylpropenes chavicol and eugenol to methylchavicol and methyleugenol, respectively. Chavicol O-methyltransferase (CVOMT) and eugenol O-methyltransferase (EOMT) cDNAs were isolated from the sweet basil variety EMX-1 using a biochemical genomics approach. These cDNAs encode proteins that are 90\% identical to each other and very similar to several isoflavone O-methyltransferases such as IOMT, which catalyzes the 4{\textquoteright}-O-methylation of 2,7,4{\textquoteright}-trihydroxyisoflavanone. On the other hand, CVOMT1 and EOMT1 are related only distantly to (iso)eugenol OMT from Clarkia breweri, indicating that the eugenol O-methylating enzymes in basil and C. breweri evolved independently. Transcripts for CVOMT1 and EOMT1 were highly expressed in the peltate glandular trichomes on the surface of the young basil leaves. The CVOMT1 and EOMT1 cDNAs were expressed in Escherichia coli, and active proteins were produced. CVOMT1 catalyzed the O-methylation of chavicol, and EOMT1 also catalyzed the O-methylation of chavicol with equal efficiency to that of CVOMT1, but it was much more efficient in O-methylating eugenol. Molecular modeling, based on the crystal structure of IOMT, suggested that a single amino acid difference was responsible for the difference in substrate discrimination between CVOMT1 and EOMT1. This prediction was confirmed by site-directed mutagenesis, in which the appropriate mutants of CVOMT1 (F260S) and EOMT1 (S261F) were produced that exhibited the opposite substrate preference relative to the respective native enzyme.},
	keywords = {Amino Acid Sequence, Anisoles, DNA: Complementary, Escherichia coli, Eugenol, Evolution: Molecular, Gene Expression, Gene Expression Regulation: Enzymologic, Gene Expression Regulation: Plant, Isoflavones, Methyltransferases, Molecular Sequence Data, Molecular Structure, Mutagenesis: Site-Directed, Mutation, Ocimum basilicum, Phylogeny, Recombinant Proteins, Sequence Homology: Amino Acid, Substrate Specificity},
	author = {David R Gang and Noa Lavid and Chloe Zubieta and Feng Chen and Till Beuerle and Efraim Lewinsohn and Joseph P Noel and Eran Pichersky}
}
@article {Iijima:2004p8022,
	title = {The biochemical and molecular basis for the divergent patterns in the biosynthesis of terpenes and phenylpropenes in the peltate glands of three cultivars of basil},
	journal = {Plant Physiol},
	volume = {136},
	number = {3},
	year = {2004},
	month = {Nov},
	pages = {3724{\textendash}36},
	abstract = {Surface glandular trichomes distributed throughout the aerial parts of sweet basil (Ocimum basilicum) produce and store monoterpene, sesquiterpene, and phenylpropene volatiles. Three distinct basil chemotypes were used to examine the molecular mechanisms underlying the divergence in their monoterpene and sesquiterpene content. The relative levels of specific terpenes in the glandular trichomes of each cultivar were correlated with the levels of transcripts for eight genes encoding distinct terpene synthases. In a cultivar that produces mostly (R)-linalool, transcripts of (R)-linalool synthase (LIS) were the most abundant of these eight. In a cultivar that synthesizes mostly geraniol, transcripts of geraniol synthase were the most abundant, but the glands of this cultivar also contained a transcript of an (R)-LIS gene with a 1-base insertion that caused a frameshift mutation. A geraniol synthase-LIS hybrid gene was constructed and expressed in Escherichia coli, and the protein catalyzed the formation of both geraniol and (R)-linalool from geranyl diphosphate. The total amounts of terpenes were correlated with total levels of terpene synthase activities, and negatively correlated with levels of phenylpropanoids and phenylalanine ammonia lyase activity. The relative levels of geranyl diphosphate synthase and farnesyl diphosphate synthase activities did not correlate with the total amount of terpenes produced, but showed some correlation with the ratio of monoterpenes to sesquiterpenes.},
	keywords = {Amino Acid Sequence, Gene Expression Regulation: Plant, Genetic Variation, Molecular Sequence Data, Molecular Structure, Ocimum basilicum, Phylogeny, Sequence Homology: Amino Acid, Styrenes, Terpenes},
	doi = {10.1104/pp.104.051318},
	author = {Yoko Iijima and Rachel Davidovich-Rikanati and Eyal Fridman and David R Gang and Einat Bar and Efraim Lewinsohn and Eran Pichersky}
}
@article {TapernouxLuthi:2004p8016,
	title = {Cloning, functional expression, and characterization of the raffinose oligosaccharide chain elongation enzyme, galactan:galactan galactosyltransferase, from common bugle leaves},
	journal = {Plant Physiol},
	volume = {134},
	number = {4},
	year = {2004},
	month = {Apr},
	pages = {1377{\textendash}87},
	abstract = {Galactan:galactan galactosyltransferase (GGT) is a unique enzyme of the raffinose family oligosaccharide (RFO) biosynthetic pathway. It catalyzes the chain elongation of RFOs without using galactinol (alpha-galactosyl-myoinositol) by simply transferring a terminal alpha-galactosyl residue from one RFO molecule to another one. Here, we report the cloning and functional expression of a cDNA encoding GGT from leaves of the common bugle (Ajuga reptans), a winter-hardy long-chain RFO-storing Lamiaceae. The cDNA comprises an open reading frame of 1215 bp. Expression in tobacco (Nicotiana plumbaginifolia) protoplasts resulted in a functional recombinant protein, which showed GGT activity like the previously described purified, native GGT enzyme. At the amino acid level, GGT shows high homologies (>60\%) to acid plant alpha-galactosidases of the family 27 of glycosylhydrolases. It is clearly distinct from the family 36 of glycosylhydrolases, which harbor galactinol-dependent raffinose and stachyose synthases as well as alkaline alpha-galactosidases. Physiological studies on the role of GGT confirmed that GGT plays a key role in RFO chain elongation and carbon storage. When excised leaves were exposed to chilling temperatures, levels of GGT transcripts, enzyme activities, and long-chain RFO concentrations increased concomitantly. On a whole-plant level, chilling temperatures induced GGT expression mainly in the roots and fully developed leaves, both known RFO storage organs of the common bugle, indicating an adaptation of the metabolism from active growth to transient storage in the cold.},
	keywords = {Ajuga, Amino Acid Sequence, Cloning: Molecular, Cold Temperature, DNA: Complementary, Galactosyltransferases, Gene Expression Regulation: Enzymologic, Gene Expression Regulation: Plant, Molecular Sequence Data, Phylogeny, Plant Leaves, Plant Proteins, Raffinose, Sequence Analysis: DNA, Sequence Homology: Amino Acid, Tobacco},
	doi = {10.1104/pp.103.036210},
	author = {Esther M Tapernoux-L{\"u}thi and Andreas B{\"o}hm and Felix Keller}
}
@article {Zhou:2008p7979,
	title = {Altered expression patterns of TCP and MYB genes relating to the floral developmental transition from initial zygomorphy to actinomorphy in Bournea (Gesneriaceae)},
	journal = {New Phytol},
	volume = {178},
	number = {3},
	year = {2008},
	month = {Jan},
	pages = {532{\textendash}43},
	abstract = {The shift from zygomorphy to actinomorphy has been intensively studied in molecular genetic model organisms. However, it is still a key challenge to explain the great morphological diversity of derived actinomorphy in angiosperms, since different underlying mechanisms may be responsible for similar external morphologies. Bournea (Gesneriaceae) is of particular interest in addressing this question, as it is a representative of primarily derived actinomorphy characteristic of a unique developmental transition from zygomorphy to actinomorphic flowers at anthesis. Using RNA in situ hybridization, the expression patterns were investigated of three different Bournea orthologues of TCP and MYB genes that have been shown to control floral symmetry in model species. Here, it is shown that the initial zygomorphic pattern in Bournea is likely a residual zygomorphy resulting from conserved expression of the adaxial (dorsal) identity gene BlCYC1. As a key novel event, the late downregulation of BlCYC1 and BlRAD and the correlative changes in the late specific expression of the abaxial (ventral) identity gene BlDIV should be responsible for the origin of the derived actinomorphy in Bournea. These results further indicate that there might be diverse pathways in the origin and evolution of derived actinomorphy through modifications of pre-existing zygomorphic developmental programs under dynamics of regulatory networks.},
	keywords = {Flowers, Gene Expression Regulation: Plant, Genes: Plant, Lamiaceae, Phylogeny, Plant Proteins},
	doi = {10.1111/j.1469-8137.2008.02384.x},
	author = {Xiu-Ren Zhou and Yin-Zheng Wang and James F Smith and Rujin Chen}
}
@article {Kitada:2001p8039,
	title = {Differential expression of two cytochrome P450s involved in the biosynthesis of flavones and anthocyanins in chemo-varietal forms of Perilla frutescens},
	journal = {Plant Cell Physiol},
	volume = {42},
	number = {12},
	year = {2001},
	month = {Dec},
	pages = {1338{\textendash}44},
	abstract = {In Perilla frutescens, there are two varietal forms of anthocyanin accumulation, i.e. red and green forms. The cDNA clones encoding flavone synthase II (FSII) and flavonoid 3{\textquoteright}-hydroxylase (F3{\textquoteright}H), two cytochrome P450s that are involved in the biosynthesis of flavones and anthocyanins, were isolated from P. frutescens. The FSII cDNA encoded a 57.1 kDa protein designated as CYP93B6, and the F3{\textquoteright}H cDNA encoded 57.5 kDa protein designated as CYP75B4. Recombinant CYP93B6 expressed in yeast converted flavanones to flavones with K(m) values of 8.8-11.9 microM. Recombinant CYP75B4 catalyzed 3{\textquoteright}-hydroxylation of flavanones to the corresponding compounds with K(m) values of 18-20 microM. The CYP93B6 transcript accumulated to an equal level in leaves of both red and green forms of P. frutescens, in agreement with the accumulation pattern of flavones in the leaves. However, the CYP75B4 transcript was predominantly expressed in the red form of P. frutescens, and its expression was induced by light in conjunction with other transcripts of biosynthetic enzymes of anthocyanin. These results indicate that gene expression of a set of anthocyanin biosynthetic enzymes including F3{\textquoteright}H is regulated coordinately only in the red form of P. frutescens but not in the green form, whilst FSII gene expression is controlled in a similar manner in red and green forms of P. frutescens.},
	keywords = {Anthocyanins, Apigenin, Cytochrome P-450 Enzyme System, Flavonoids, Gene Expression Regulation: Enzymologic, Gene Expression Regulation: Plant, Kinetics, Lamiaceae, Luteolin, Mixed Function Oxygenases, Phylogeny, Plant Structures},
	author = {C Kitada and Z Gong and Y Tanaka and M Yamazaki and K Saito}
}
