Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor

@inproceedings{Huijbers2017ProlineDF,
  title={Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor},
  author={Mieke M. E. Huijbers and Marta Mart{\'i}nez-J{\'u}lvez and Adrie H. Westphal and Estela Delgado-Arciniega and Milagros Medina and Willem J H van Berkel},
  booktitle={Scientific reports},
  year={2017}
}
Flavoenzymes are versatile biocatalysts containing either FAD or FMN as cofactor. FAD often binds to a Rossmann fold, while FMN prefers a TIM-barrel or flavodoxin-like fold. Proline dehydrogenase is denoted as an exception: it possesses a TIM barrel-like fold while binding FAD. Using a riboflavin auxotrophic Escherichia coli strain and maltose-binding protein as solubility tag, we produced the apoprotein of Thermus thermophilus ProDH (MBP-TtProDH). Remarkably, reconstitution with FAD or FMN… CONTINUE READING
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