Poppies provide missing piece of morphine biosynthesis puzzle

June 25, 2015

Researchers studying poppy plants -- the natural source of pain-relieving alkaloids, such as morphine and codeine -- have identified a fusion gene that facilitates important, back-to-back steps in the plant's morphine-producing pathway. These findings, which build upon recent efforts to engineer the morphine biosynthesis pathway in yeast, complete the metabolic pathway for morphine and pave the way for cheaper, safer routes to producing the economically important drug without the need for cultivating poppy fields. For about a decade, researchers have been trying to put genes into yeast that would allow the microbes to synthesize morphine. Until now, researchers interested in this process had been searching for an enzyme in the morphine biosynthesis pathway that reconfigures the compound known as (S)-reticuline into a variation called (R)-reticuline. By studying mutations in the poppy plant Papaver somniferum, Thilo Winzer and colleagues discovered that the STORR enzyme, expressed by a gene of the same name, catalyzed two related steps, converting (S)-reticuline to an amine, known as 1,2-dehydroreticuline, and then converting that intermediate substrate to (R)-reticuline. The STORR enzyme contains a cytochrome P450 module, which facilitates the first step of the process, along with oxidoreductase modules that facilitate the second step, according to the researchers. Now that the biosynthetic pathway to morphine is complete, researchers can investigate more efficient, microbial-based approaches to opiate-based pain-relievers, which generate billions of dollars in sales each year.
Article #25: "Morphinan biosynthesis in opium poppy requires a P450-oxidoreductase fusion protein," by T. Winzer; M. Kern; A.J. King; T.R. Larson; R. Teodor; S. Donninger; Y. Li; A.A. Dowle; J. Cartwright; R. Bates; D. Ashford; J. Thomas; I.A. Graham at University of York in York, UK; C. Walker; T.A. Bowser at GlaxoSmithKline in Boronia, VIC, Australia.

American Association for the Advancement of Science

Related Enzyme Articles from Brightsurf:

Repairing the photosynthetic enzyme Rubisco
Researchers at the Max Planck Institute of Biochemistry decipher the molecular mechanism of Rubisco Activase

Oldest enzyme in cellular respiration isolated
Researchers from Goethe University have found what is perhaps the oldest enzyme in cellular respiration.

UQ researchers solve a 50-year-old enzyme mystery
Advanced herbicides and treatments for infection may result from the unravelling of a 50-year-old mystery by University of Queensland researchers.

Overactive enzyme causes hereditary hypertension
After more than 40 years, several teams at the MDC and ECRC have now made a breakthrough discovery with the help of two animal models: they have proven that an altered gene encoding the enzyme PDE3A causes an inherited form of high blood pressure.

Triggered by light, a novel way to switch on an enzyme
In living cells, enzymes drive biochemical metabolic processes. It is this very ability which allows them to be used as catalysts in biotechnology, for example to create chemical products such as pharmaceutics.

A 'corset' for the enzyme structure
The structure of enzymes determines how they control vital processes such as digestion or immune response.

Could inhibiting the DPP4 enzyme help treat coronavirus?
Researchers and clinicians are scrambling to find ways to combat COVID-19, including new therapeutics and eventually a vaccine.

Bacterial enzyme could become a new target for antibiotics
Scientists discover the structure of an enzyme, found in the human gut, that breaks down a component of collagen.

Chemists create new artificial enzyme
Rajeev Prabhakar, a computational chemist at the University of Miami, and his collaborators at the University of Michigan have created a novel, synthetic, three-stranded molecule that functions just like a natural metalloenzyme, or an enzyme that contains metal ions.

First artificial enzyme created with two non-biological groups
Scientists at the University of Groningen turned a non-enzymatic protein into a new, artificial enzyme by adding two abiological catalytic components: an unnatural amino acid and a catalytic copper complex.

Read More: Enzyme News and Enzyme Current Events
Brightsurf.com is a participant in the Amazon Services LLC Associates Program, an affiliate advertising program designed to provide a means for sites to earn advertising fees by advertising and linking to Amazon.com.