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The π‐helix located at the tetramer interface of two‐component FMN‐dependent reductases contributes to the structural divergence from canonical FMN‐bound reductases within the NADPH:FMN reductase family. The π‐helix in the SsuE FMN‐dependent reductase of the alkanesulfonate monooxygenase system has been proposed to be generated by the insertion of a Tyr residue in the conserved α4‐helix. Variants...
The Aspergillus fumigatus old yellow enzyme (OYE) EasA reduces chanoclavine‐I aldehyde to dihydrochanoclavine aldehyde and works in conjunction with festuclavine synthase at the branchpoint for ergot alkaloid pathways. The crystal structure of the FMN‐loaded EasA was determined to 1.8 Å resolution. The active‐site amino acids of OYE are conserved, supporting a similar mechanism for reduction of the...
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