@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 {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}
}
