1qyd
From Proteopedia
Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases, and their relationship to isoflavone reductases
Structural highlights
FunctionPILR1_THUPL Reductase involved in lignan biosynthesis. Catalyzes the enantioselective sequential conversion of (-)-pinoresinol into (-)-lariciresinol and of (-)-lariciresinol into (+)-secoisolariciresinol. Can also convert with a lower efficiency (+)-pinoresinol into (+)-lariciresinol, but not (+)-lariciresinol into (-)-secoisolariciresinol. Abstracts the 4R-hydride from the NADPH cofactor during catalysis.[1] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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Categories: Large Structures | Thuja plicata | Bedgar DL | Davin LB | Gang DR | Halls SC | Hilsenbeck JL | Kang C | Kasahara H | Lawrence PK | Min T | Park H | Youn B