Abstract
A concise and efficient total synthesis of the lignan natural product larreatricin as well as an unambiguous assignment of configuration of its enantiomers are reported, resolving a long‐held controversy. Enzyme kinetic studies revealed that different polyphenol oxidases show high and remarkably divergent enantioselective recognition of this secondary metabolite.
Highlights
Chirality is a ubiquitous feature of biological systems that plays a critical role in the metabolic processes of living organisms.[1]
The best characterized Polyphenol oxidases (PPOs) are those from mushrooms, among which AbPPO4[11] is reported to preferentially convert l-tyrosine over d-tyrosine.[11a]. The enantiospecificity of PPOs or how PPOs select one enantiomer of a substrate over the other remain poorly investigated
We report detailed kinetic studies of its divergent enantiospecific uptake by three different tyrosinases from two kingdoms (Scheme 1 C„ Table 1), including (+)-larreatricin hydroxylase, which we were able to produce recombinantly for the first time
Summary
Chirality is a ubiquitous feature of biological systems that plays a critical role in the metabolic processes of living organisms.[1].
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