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Eschscholzia califomica

Frias L. D., Godoy, R., Iturra, P., Koref-Santibanez, S., Navarro, J., Pacheco, N. and Stebbins, G. L. 1975. Polymorphism and geographic variation in flower color in Chilean populations of Eschscholzia califomica. Plant Syst. Evol. 123 185-198. [Pg.312]

Magnoflorine Coptis japonica Corydalis incisa Eschscholzia califomica Fumaria capreolata Papaver bracteatum Papaver somniferum Thalictrum minus... [Pg.200]

Sanguinarine Chelidonium majus Corydalis ophiocarpa Eschscholzia califomica Fumaria cordata Macleaya cordata... [Pg.201]

HAUSCHILD, K., PAULI, H.H., KUTCHAN, T.M., Isolation and analysis of a gene bbel encoding the berberine bridge enzyme from the California poppy Eschscholzia califomica. Plant Mol. Biol., 1998,36,473-478. [Pg.170]

The isoquinoline alkaloids include the analgesics morphine and codeine as well as the antibiotic berberine (Fig. la). Morphine and codeine are two of the most important analgesics used in medicine, and plants remain the main commercial source of the alkaloids (8). Development of plant cell cultures of Eschscholzia califomica, Papaver somniferum, and Coptis japonica has aided in the isolation and cloning of many enzymes involved in the biosynthesis of isoquinoline alkaloids (9). [Pg.1]

Jain L, Tripathi M, Pandey VB. Alkaloids of Eschscholzia califomica. Planta Med 1996 62 188. [Pg.82]

Ikezawa, N., K. Iwasa, and F. Sato, Molecular cloning and characterization of methylenedioxy bridge-forming enzymes involved in stylopine biosynthesis in Eschscholzia califomica. FEBSJ., 2007. 274(4) p. 1019-35. [Pg.74]

Takemura, T., et al.. Molecular cloning and characterization of a cytochrome P450 in sanguinarine biosynthesis from Eschscholzia califomica cells. Phytochemistry, 2013. 91 p. 100-8. [Pg.74]

The berberine bridge enzyme utilized in tet-rahydroisoquinoline alkaloid pathways was cloned by this method [19]. This enzyme was purified from elicited Eschscholzia califomica cell suspension cultures in six to seven steps, where approximately 10 pg of pure protein was obtained from 700 mg of crude protein. The purified protein was digested with trypsin and the resulting peptides were subjected to N-terminal sequencing. An oligonucleotide primer based on one of these amino acid sequences was shown to hybridize to a clone Irom an E. califomica cDNA library. This clone was sequenced and shown to encode the amino acid sequences observed by N-terminal sequencing of the purified protein. The clone was then het-erologously expressed in S. cerevisea and was shown to catalyze the expected biochemical activity - formation of (5)-reticuline to (S)-scoulerine - as evidenced by a number of spectroscopic characterizations. [Pg.168]

Anthriscus sylvestris Aethusa cynapium Aphanes arvensis Sagina procumbens Thlaspi arvense Persicaria lapathifolia Matricaria disciodes Plantago major P. lanceolata Papaver rhoeas Eschscholzia califomica Primula vulgaris... [Pg.537]

The BBE from Eschscholzia califomica (California poppy) is the best-characterized member of this enzyme class due to the availability of an efficient heterologous expression system using Pichia pastoris [158,159]. Moreover, its biochemical properties, structure, and reaction mechanism were thoroughly investigated [160-162]. In addition, the potential of BBE was investigated for biocatalytic applications such as the kinetic resolution of different racemic nonnatural benzylisoquinolines [16,163,164]. [Pg.50]


See other pages where Eschscholzia califomica is mentioned: [Pg.291]    [Pg.291]    [Pg.165]    [Pg.22]    [Pg.176]    [Pg.61]    [Pg.444]    [Pg.254]    [Pg.261]    [Pg.131]   
See also in sourсe #XX -- [ Pg.291 ]

See also in sourсe #XX -- [ Pg.61 ]




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