Journal
PHYTOCHEMISTRY REVIEWS
Volume 17, Issue 2, Pages 249-277Publisher
SPRINGER
DOI: 10.1007/s11101-017-9519-z
Keywords
Benzylisoquinoline alkaloid; Enzyme family; Specialized metabolism; Cytochrome P450; FAD-linked oxidoreductase; NADPH-dependent reductase; Acetyl-CoA-dependent acetyltransferase; Carboxylesterase; Pathogenesis-related protein 10
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Funding
- Natural Sciences and Engineering Research Council of Canada
- University of Calgary Eyes High Postdoctoral Scholarship
- Natural Sciences and Engineering Reserach Council of Canada
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Benzylisoquinoline alkaloids (BIAs) are a group of specialized metabolites found predominantly in the plant order Ranunculales. Approximately 2500 naturally occurring BIAs have been identified, many of which possess a variety of potent biological and pharmacological properties. The initial BIA skeleton is formed via condensation by a unique enzyme, norcoclaurine synthase, of the L-tyrosine derivatives dopamine and 4-hydroxyphenylacetaldehyde, yielding (S)-norcoclaurine as a central intermediate. The vast diversity of BIA structures is subsequently derived from (1) transformation of the basic BIA backbone by oxidative enzymes, particularly cytochromes P450 and FAD-linked oxidases, and (2) further structural and functional group modification by tailoring enzymes, which also include various reductases, dioxygenases, acetyltransferases, and carboxylesterases. Most of the biosynthetic enzymes responsible for the biosynthesis of major BIAs (i.e. morphine, noscapine, papaverine, and sanguinarine) in opium poppy (Papaver somniferum), and other compounds (e.g. berberine) in related plants, have been isolated and partially characterized. Diversity in BIA metabolism is driven by the modular and repetitive recruitment, and subsequent neo-functionalization, of a limited number of ancestral enzymes. In this review, BIA biosynthetic enzymes are discussed in the context of their respective families, facilitating exploration of common phylogeny and biochemical mechanisms.
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