@article {Yamazaki:1999p8037,
	title = {Molecular cloning and biochemical characterization of a novel anthocyanin 5-O-glucosyltransferase by mRNA differential display for plant forms regarding anthocyanin},
	journal = {J Biol Chem},
	volume = {274},
	number = {11},
	year = {1999},
	month = {Mar},
	pages = {7405{\textendash}11},
	abstract = {UDP-glucose: anthocyanin 5-O-glucosyltransferase (5-GT) is responsible for the modification of anthocyanins to more stable molecules in complexes for co-pigmentation, supposedly resulting in a purple hue. The cDNA encoding 5-GT was isolated by a differential display applied to two different forms of anthocyanin production in Perilla frutescens var. crispa. Differential display was carried out for mRNA from the leaves of reddish-purple and green forms of P. frutescens, resulting in the isolation of five cDNA clones predominantly expressed in the red form. The cDNA encoded a polypeptide of 460 amino acids, exhibiting a low homology with the sequences of several glucosyltransferases including UDP-glucose: anthocyanidin 3-O-glucosyltransferase. By using this cDNA as the probe, we also isolated a homologous cDNA clone from a petal cDNA library of Verbena hybrida. To identify the biochemical function of the encoded proteins, these cDNAs were expressed in Saccharomyces cerevisiae cells. The recombinant proteins in the yeast extracts catalyzed the conversion of anthocyanidin 3-O-glucosides into the corresponding anthocyanidin 3,5-di-O-glucosides using UDP-glucose as a cofactor, indicating the identity of the cDNAs encoding 5-GT. Several biochemical properties (optimum pH, Km values, and sensitivity to inhibitors) were similar to those reported previously for 5-GTs. Southern blot analysis indicated the presence of two copies of 5-GT genes in the genome of both red and green forms of P. frutescens. The mRNA accumulation of the 5-GT gene was detected in the leaves of the red form but not in those of the green form and was induced by illumination of light, as observed for other structural genes for anthocyanin biosynthesis in P. frutescens.},
	keywords = {Amino Acid Sequence, Anthocyanins, Cloning: Molecular, DNA: Complementary, Glucosyltransferases, Lamiaceae, Molecular Sequence Data, Phylogeny, Recombinant Proteins, RNA: Messenger, Saccharomyces cerevisiae, Sequence Homology: Amino Acid},
	author = {M Yamazaki and Z Gong and M Fukuchi-Mizutani and Y Fukui and Y Tanaka and T Kusumi and K Saito}
}
@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 {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 {Berger:2006p7995,
	title = {Rosmarinic acid synthase is a new member of the superfamily of BAHD acyltransferases},
	journal = {Planta},
	volume = {224},
	number = {6},
	year = {2006},
	month = {Nov},
	pages = {1503{\textendash}10},
	abstract = {Purification of rosmarinic acid synthase (hydroxycinnamoyl-CoA:hydroxyphenyllactate hydroxycinnamoyltransferase) from suspension cells of Coleus blumei Benth. (Lamiaceae) by fractionated ammonium sulphate precipitation, hydrophobic interaction chromatography and two affinity chromatography steps led to the identification of peptide sequences, which enabled a PCR-based approach to isolate the full-length cDNA encoding this enzyme. The open reading frame of the cDNA had a length of 1290 base pairs encoding a protein of 430 amino acid residues with a molecular mass of 47,932 Da with typical characteristics of an acyltransferase of the BAHD superfamily. The cDNA was heterologously expressed in Escherichia coli. The enzyme displayed the activity of rosmarinic acid synthase using 4-coumaroyl- and caffeoyl-coenzyme A and 4-hydroxyphenyllactate as well as 3.4-dihydroxyphenyllactate as substrates. Shikimic acid and quinic acid were not able to serve as hydroxycinnamoyl acceptors. This therefore is the first report of the cDNA-cloning of a rosmarinic acid synthase.},
	keywords = {Acyltransferases, Amino Acid Sequence, Base Sequence, DNA: Complementary, Molecular Sequence Data, Phylogeny, Polymerase Chain Reaction},
	doi = {10.1007/s00425-006-0393-y},
	author = {Anja Berger and Juliane Meinhard and Maike Petersen}
}
@article {Hosoi:2004p8023,
	title = {cDNA isolation and functional expression of myrcene synthase from Perilla frutescens},
	journal = {Biol Pharm Bull},
	volume = {27},
	number = {12},
	year = {2004},
	month = {Dec},
	pages = {1979{\textendash}85},
	abstract = {cDNA cloning of a monoterpene synthase from Perilla frutescens whose steam-distilled oil contains 92.9\% perillaketone, was performed by the PCR method using primers designed based on limonene synthase. The full-length nucleotide sequence of this cDNA consisted of 1978 bp including a 1827-bp translational region encoding a deduced protein of 608 amino acids, which was similar to that of limonene synthase from P. frutescens (85\% identity). Functional expression of this clone in Escherichia coli yielded an active monoterpene synthase enzyme, which converted geranyl diphosphate into 53.8\% myrcene, 20.9\% sabinene, 19.8\% linalool and 5.5\% limonene. As for the extraction of reaction products, we performed SPME (solid phase micro extraction) as well as conventional solvent extraction, and compared these two extraction methods.},
	keywords = {Amino Acid Sequence, DNA: Complementary, Gene Expression Regulation: Enzymologic, Intramolecular Lyases, Molecular Sequence Data, Perilla frutescens, Phylogeny},
	author = {Madoka Hosoi and Michiho Ito and Toru Yagura and Robert Phillip Adams and Gisho Honda}
}
@article {Matsuno:2002p8029,
	title = {CYP98A6 from Lithospermum erythrorhizon encodes 4-coumaroyl-4{\textquoteright}-hydroxyphenyllactic acid 3-hydroxylase involved in rosmarinic acid biosynthesis},
	journal = {FEBS Lett},
	volume = {514},
	number = {2-3},
	year = {2002},
	month = {Mar},
	pages = {219{\textendash}24},
	abstract = {Rosmarinic acid is the dominant hydroxycinnamic acid ester accumulated in Boraginaceae and Lamiaceae plants. A cytochrome P450 cDNA was isolated by differential display from cultured cells of Lithospermum erythrorhizon, and the gene product was designated CYP98A6 based on the deduced amino acid sequence. After expression in yeast, the P450 was shown to catalyze the 3-hydroxylation of 4-coumaroyl-4{\textquoteright}-hydroxyphenyllactic acid, one of the final two steps leading to rosmarinic acid. The expression level of CYP98A6 is dramatically increased by addition of yeast extract or methyl jasmonate to L. erythrorhizon cells, and its expression pattern reflected the elicitor-induced change in rosmarinic acid production, indicating that CYP98A6 plays an important role in regulation of rosmarinic acid biosynthesis.},
	keywords = {Acetates, Cell Extracts, Cells: Cultured, Cinnamates, Cloning: Molecular, Cyclopentanes, Cytochrome P-450 Enzyme System, Depsides, DNA: Complementary, Gene Expression, Gene Expression Profiling, Lithospermum, Mixed Function Oxygenases, Molecular Sequence Data, Oxylipins, Phenylalanine Ammonia-Lyase, Phenylpropionates, Phylogeny, Plant Proteins, RNA: Messenger},
	author = {Michiyo Matsuno and Akito Nagatsu and Yukio Ogihara and Brian E Ellis and Hajime Mizukami}
}
@article {Iijima:2004p8034,
	title = {Characterization of geraniol synthase from the peltate glands of sweet basil},
	journal = {Plant Physiol},
	volume = {134},
	number = {1},
	year = {2004},
	month = {Jan},
	pages = {370{\textendash}9},
	abstract = {The monoterpene fraction of the lemon-scented sweet basil (Ocimum basilicum) cv Sweet Dani consists mostly of citral (a mixture of geranial and neral), with lower levels of geraniol and nerol. These compounds are stored in the peltate glands found on the leaf epidermis. Younger leaves, which have a higher density of such glands, also have a higher content of monoterpenes than older leaves. Geraniol synthase (GES) activity, generating geraniol from geranyl diphosphate, was shown to be localized exclusively or almost exclusively to glands. GES activity resides in a homodimeric protein that was purified to near homogeneity. Basil GES requires Mn2+ as a divalent metal cofactor for activity and produces only geraniol from geranyl diphosphate. Km values of 21 and 51 microM were obtained for geranyl diphosphate and Mn2+, respectively. In the presence of 18O-labeled water, GES catalyzed the formation of 18O-geraniol from geranyl diphosphate, indicating that the reaction mechanism of GES is similar to that of other monoterpene synthases and is different from the action of phosphatases. A GES cDNA was isolated based on analysis of a glandular trichome expressed sequence tag database, and the sequence of the protein encoded by this cDNA shows some similarity to sequences of other terpene synthases. The expression of the GES cDNA in Escherichia coli resulted in a protein with enzymatic activity essentially identical to that of plant-purified GES. RNA gel-blot analysis indicated that GES is expressed in glands but not in leaves of basil cv Sweet Dani, whose glands contain geraniol and citral, and not in glands or leaves of another basil variety that makes other monoterpenes but not geraniol or citral.},
	keywords = {Alkyl and Aryl Transferases, Amino Acid Sequence, DNA: Complementary, DNA: Plant, Gene Expression, Genes: Plant, Molecular Sequence Data, Ocimum basilicum, Phylogeny, Plant Structures, Sequence Homology: Amino Acid, Terpenes},
	doi = {10.1104/pp.103.032946},
	author = {Yoko Iijima and David R Gang and Eyal Fridman and Efraim Lewinsohn and Eran Pichersky}
}
