ArticleThe Journal of biological chemistry2009
Removal of substrate inhibition and increase in maximal velocity in the short chain dehydrogenase/reductase salutaridine reductase involved in morphine biosynthesis.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 39 citations in OpenAlex.
- Advances in the biosynthesis of naturally occurring benzylisoquinoline alkaloids.Frontiers in plant science · 2025Review
- Structural Characterization and Molecular Dynamics Study of the REPI Fusion Protein fromBiomolecules · 2023Article
- Acceptors and Effectors Alter Substrate Inhibition Kinetics of a Plant Glucosyltransferase NbUGT72AY1 and Its Mutants.International journal of molecular sciences · 2023Article
- High level expression of nicotinamide nucleoside kinase fromFrontiers in bioengineering and biotechnology · 2023Article
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- Biosynthesis and synthetic biology of psychoactive natural products.Chemical Society reviews · 2021Review
- Multiple mechanisms contribute to increased neutral lipid accumulation in yeast producing recombinant variants of plant diacylglycerol acyltransferase 1.The Journal of biological chemistry · 2017Article
- Yeast factories for the production of aromatic compounds: from building blocks to plant secondary metabolites.Journal of industrial microbiology & biotechnology · 2016Review
- Complete biosynthesis of opioids in yeast.Science (New York, N.Y.) · 2015Article
- Article
- Crystal structure of a lipoxygenase in complex with substrate: the arachidonic acid-binding site of 8R-lipoxygenase.The Journal of biological chemistry · 2014Article
- Structure-based mutational studies of substrate inhibition of betaine aldehyde dehydrogenase BetB from Staphylococcus aureus.Applied and environmental microbiology · 2014Article
- Dioxygenases catalyze O-demethylation and O,O-demethylenation with widespread roles in benzylisoquinoline alkaloid metabolism in opium poppy.The Journal of biological chemistry · 2013Article
- Atomic structure of salutaridine reductase from the opium poppy (Papaver somniferum).The Journal of biological chemistry · 2011Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Salutaridine reductase (SalR, EC 1.1.1.248) catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine. It belongs to a new, plant-specific class of short-chain dehydrogenases, which are characterized by their monomeric nature and increased length compared with related enzymes. Homology modeling and substrate docking suggested that additional amino acids form a novel alpha-helical element, which is involved in substrate binding. Site-directed mutagenesis and subsequent studies on enzyme kinetics revealed the importance of three residues in this element for substrate binding. Further replacement of eight additional residues led to the characterization of the entire substrate binding pocket. In addition, a specific role in salutaridine binding by either hydrogen bond formation or hydrophobic interactions was assigned to each amino acid. Substrate docking also revealed an alternative mode for salutaridine binding, which could explain the strong substrate inhibition of SalR. An alternate arrangement of salutaridine in the enzyme was corroborated by the effect of various amino acid substitutions on substrate inhibition. In most cases, the complete removal of substrate inhibition was accompanied by a substantial loss in enzyme activity. However, some mutations greatly reduced substrate inhibition while maintaining or even increasing the maximal velocity. Based on these results, a double mutant of SalR was created that exhibited the complete absence of substrate inhibition and higher activity compared with wild-type SalR.
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