@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 {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}
}
@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}
}
