@article {Ringer:2005p8013,
	title = {Monoterpene metabolism. Cloning, expression, and characterization of (-)-isopiperitenol/(-)-carveol dehydrogenase of peppermint and spearmint},
	journal = {Plant Physiol},
	volume = {137},
	number = {3},
	year = {2005},
	month = {Mar},
	pages = {863{\textendash}72},
	abstract = {The essential oils of peppermint (Mentha x piperita) and spearmint (Mentha spicata) are distinguished by the oxygenation position on the p-menthane ring of the constitutive monoterpenes that is conferred by two regiospecific cytochrome P450 limonene-3- and limonene-6-hydroxylases. Following hydroxylation of limonene, an apparently similar dehydrogenase oxidizes (-)-trans-isopiperitenol to (-)-isopiperitenone in peppermint and (-)-trans-carveol to (-)-carvone in spearmint. Random sequencing of a peppermint oil gland secretory cell cDNA library revealed a large number of clones that specified redox-type enzymes, including dehydrogenases. Full-length dehydrogenase clones were screened by functional expression in Escherichia coli using a recently developed in situ assay. A single full-length acquisition encoding (-)-trans-isopiperitenol dehydrogenase (ISPD) was isolated. The (-)-ISPD cDNA has an open reading frame of 795 bp that encodes a 265-residue enzyme with a calculated molecular mass of 27,191. Nondegenerate primers were designed based on the (-)-trans-ISPD cDNA sequence and employed to screen a spearmint oil gland secretory cell cDNA library from which a 5{\textquoteright}-truncated cDNA encoding the spearmint homolog, (-)-trans-carveol-dehydrogenase, was isolated. Reverse transcription-PCR amplification and RACE were used to acquire the remaining 5{\textquoteright}-sequence from RNA isolated from oil gland secretory cells of spearmint leaf. The full-length spearmint dehydrogenase shares >99\% amino acid identity with its peppermint homolog and both dehydrogenases are capable of utilizing (-)-trans-isopiperitenol and (-)-trans-carveol. These isopiperitenol/carveol dehydrogenases are members of the short-chain dehydrogenase/reductase superfamily and are related to other plant short-chain dehydrogenases/reductases involved in secondary metabolism (lignan biosynthesis), stress responses, and phytosteroid biosynthesis, but they are quite dissimilar (approximately 13\% identity) to the monoterpene reductases of mint involved in (-)-menthol biosynthesis. The isolation of the genes specifying redox enzymes of monoterpene biosynthesis in mint indicates that these genes arose from different ancestors and not by simple duplication and differentiation of a common progenitor, as might have been anticipated based on the common reaction chemistry and structural similarity of the substrate monoterpenes.},
	keywords = {Alcohol Oxidoreductases, Amino Acid Sequence, Cloning: Molecular, Mentha piperita, Mentha spicata, Molecular Sequence Data, Molecular Structure, Monoterpenes, Multigene Family, Oils: Volatile, Phylogeny},
	doi = {10.1104/pp.104.053298},
	author = {Kerry L Ringer and Edward M Davis and Rodney Croteau}
}
@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 {Alipieva:2003p8026,
	title = {Benzoxazinoids and iridoid glucosides from four Lamium species},
	journal = {Phytochemistry},
	volume = {64},
	number = {8},
	year = {2003},
	month = {Dec},
	pages = {1413{\textendash}7},
	abstract = {A new class of compounds for the plant family Lamiaceae, benzoxazinoids, was found in Lamium galeobdolon. From the aerial parts of the species were isolated the new 2-O-beta-D-glucopyranosyl-6-hydroxy-2H-1,4-benzoxazin-3(4H)-one (6-hydroxy blepharin) together with four known benzoxazinoids, DHBOA-Glc, blepharin, DIBOA, DIBOA-Glc, as well as harpagide, 8-O-acetyl-harpagide and salidroside. Eight known iridoid glucosides, 24-epi-pterosterone and verbascoside were isolated from Lamium amplexicaule, L. purpureum and L. garganicum. The iridoids, 5-deoxylamiol and sesamoside, as well as the phytoecdysone, 24-epi-pterosterone, were found for the first time for the genus Lamium. The phytochemical data are discussed from a systematic and evolutionary point of view.},
	keywords = {Ecdysone, Iridoids, Lamiaceae, Molecular Structure, Nuclear Magnetic Resonance: Biomolecular, Oxazines, Phylogeny, Phytosterols},
	author = {Kalina I Alipieva and Rilka M Taskova and Ljubka N Evstatieva and Nedjalka V Handjieva and Simeon S Popov}
}
@article {Suzuki:2001p8035,
	title = {Malonyl-CoA:anthocyanin 5-O-glucoside-6"{\textquoteright}-O-malonyltransferase from scarlet sage (Salvia splendens) flowers. Enzyme purification, gene cloning, expression, and characterization},
	journal = {J Biol Chem},
	volume = {276},
	number = {52},
	year = {2001},
	month = {Dec},
	pages = {49013{\textendash}9},
	abstract = {The orange to blue coloration of flowers in nature is, in most cases, provided by anthocyanins, a class of plant flavonoids, many of which are modified by malonyl group(s). However, the identity of the enzyme catalyzing the malonylation reaction remains to be established. Here, we describe for the first time the purification, characterization, and cDNA cloning of an anthocyanin malonyltransferase from scarlet sage (Salvia splendens) flowers. The purified enzyme (termed Ss5MaT1) was a monomeric 50-kDa protein catalyzing the regiospecific transfer of the malonyl group from malonyl-CoA to the 6"{\textquoteright}-hydroxyl group of the 5-glucosyl moiety of anthocyanins. Ss5MaT1 showed a k(cat) value of 7.8 s(-1) at 30 degrees C and pH 7.0 for the malonylation of bisdemalonylsalvianin (pelargonidin 3-(6"-O-caffeyl-beta-glucopyranoside)-5-beta-glucopyranoside) and K(m) values of 101 microm and 57 microm for bisdemalonylsalvianin and malonyl-CoA, respectively. p-Coumaric acid, which mimics an aromatic acyl group linked to the 3-glucosidic moiety of an anthocyanin substrate, was a competitive inhibitor with respect to the substrate. This strongly suggests that the presence of an aromatic acyl group at the 3-glucosidic moiety of anthocyanin is important for substrate recognition by the enzyme. On the basis of the partial amino acid sequences of the purified enzyme, we isolated a cDNA encoding Ss5MaT1. Ss5MaT1 consisted of 462 amino acids and shared motifs that are commonly found among members of a versatile plant acyltransferase family, which was recently shown to include numerous homologs of unknown biochemical functions. Northern blot analysis revealed that the transcripts of Ss5MaT1 were detected in petals, sepals, bracts, and red stems, in accordance with the pigment accumulation patterns. Phylogenetic analysis suggests that the aliphatic and aromatic acylations of anthocyanins are generally catalyzed by subfamily members of the plant acyltransferase family.},
	keywords = {Acyltransferases, Amino Acid Sequence, Anthocyanins, Molecular Sequence Data, Molecular Structure, Phylogeny, Pigmentation, Plant Structures, Salvia},
	doi = {10.1074/jbc.M108444200},
	author = {H Suzuki and T Nakayama and K Yonekura-Sakakibara and Y Fukui and N Nakamura and M Nakao and Y Tanaka and M A Yamaguchi and T Kusumi and T Nishino}
}
@article {Kapteyn:2007p7982,
	title = {Evolution of Cinnamate/p-coumarate carboxyl methyltransferases and their role in the biosynthesis of methylcinnamate},
	journal = {Plant Cell},
	volume = {19},
	number = {10},
	year = {2007},
	month = {Oct},
	pages = {3212{\textendash}29},
	abstract = {Methylcinnamate, which is widely distributed throughout the plant kingdom, is a significant component of many floral scents and an important signaling molecule between plants and insects. Comparison of an EST database obtained from the glandular trichomes of a basil (Ocimum basilicum) variety that produces high levels of methylcinnamate (line MC) with other varieties producing little or no methylcinnamate identified several very closely related genes belonging to the SABATH family of carboxyl methyltransferases that are highly and almost exclusively expressed in line MC. Biochemical characterization of the corresponding recombinant proteins showed that cinnamate and p-coumarate are their best substrates for methylation, thus designating these enzymes as cinnamate/p-coumarate carboxyl methyltransferases (CCMTs). Gene expression, enzyme activity, protein profiling, and metabolite content analyses demonstrated that CCMTs are responsible for the formation of methylcinnamate in sweet basil. A phylogenetic analysis of the entire SABATH family placed these CCMTs into a clade that includes indole-3-acetic acid carboxyl methyltransferases and a large number of uncharacterized carboxyl methyltransferase-like proteins from monocots and lower plants. Structural modeling and ligand docking suggested active site residues that appear to contribute to the substrate preference of CCMTs relative to other members of the SABATH family. Site-directed mutagenesis of specific residues confirmed these findings.},
	keywords = {Amino Acid Sequence, Blotting: Southern, Cinnamates, Evolution: Molecular, Expressed Sequence Tags, Gas Chromatography-Mass Spectrometry, Gene Expression Profiling, Kinetics, Methylation, Methyltransferases, Models: Molecular, Molecular Sequence Data, Molecular Structure, Ocimum basilicum, Phylogeny, Plant Proteins, Protein Isoforms, Proteomics, Reverse Transcriptase Polymerase Chain Reaction, Sequence Homology: Amino Acid, Substrate Specificity},
	doi = {10.1105/tpc.107.054155},
	author = {Jeremy Kapteyn and Anthony V Qualley and Zhengzhi Xie and Eyal Fridman and Natalia Dudareva and David R Gang}
}
