@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 {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}
}
