Crystallization and preliminary X-ray diffraction analysis of salutaridine reductase from the opium poppy Papaver somniferum.
作者信息
Higashi Yasuhiro, Smith Thomas J, Jez Joseph M, Kutchan Toni M
机构信息
Donald Danforth Plant Science Center, 975 North Warson Road, St Louis, Missouri 63132, USA.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):163-6. doi: 10.1107/S174430910904932X. Epub 2010 Jan 27.
Abstract
The opium poppy Papaver somniferum is the source of the narcotic analgesics morphine and codeine. Salutaridine reductase (SalR; EC 1.1.1.248) reduces the C-7 keto group of salutaridine to the C-7 (S)-hydroxyl group of salutaridinol in the biosynthetic pathway that leads to morphine in the opium poppy plant. P. somniferum SalR was overproduced in Escherichia coli and purified using cobalt-affinity and size-exclusion chromatography. Hexagonal crystals belonging to space group P6(4)22 or P6(2)22 were obtained using ammonium sulfate as precipitant and diffracted to a resolution of 1.9 A.
摘要
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