Morphinan biosynthesis in opium poppy requires a P450-oxidoreductase fusion protein

Author:

Winzer Thilo1,Kern Marcelo1,King Andrew J.1,Larson Tony R.1,Teodor Roxana I.1,Donninger Samantha L.1,Li Yi1,Dowle Adam A.2,Cartwright Jared2,Bates Rachel2,Ashford David2,Thomas Jerry2,Walker Carol3,Bowser Tim A.3,Graham Ian A.1

Affiliation:

1. Centre for Novel Agricultural Products, Department of Biology, University of York, York YO10 5DD, UK.

2. Bioscience Technology Facility, Department of Biology, University of York, York YO10 5DD, UK.

3. GlaxoSmithKline, 1061 Mountain Highway, Post Office Box 168, Boronia, Victoria 3155, Australia.

Abstract

Substrate channeling in morphine biosynthesis Poppies are still the most economically viable source of the excellent painkiller morphine. Winzer et al. have now identified a key enzyme in the poppy's biosynthetic pathway for morphine. The enzyme turns out to be an unusual protein that contains both cytochrome P-450 and oxidoreductase modules. Together these modules process two subsequent steps in the biosynthetic pathway. The identification of this enzyme may enable alternate routes for morphine biosynthesis that are less dependent on poppy cultivation. Science , this issue p. 309

Funder

UK Biotechnology and Biological Sciences Research Council

The Garfield Weston Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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