Crystal structures of putative flavin dependent monooxygenase from Alicyclobacillus acidocaldarius

Hyunjin Moon, Sungwook Shin, Jungwoo Choe

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


Flavin dependent monooxygenases catalyze various reactions to play a key role in biological processes, such as catabolism, detoxification, and biosynthesis. Group D flavin dependent monooxygenases are enzymes with an Acyl-CoA dehydrogenase (ACAD) fold and use Flavin adenine dinucleotide (FAD) or Flavin mononucleotide (FMN) as a cofactor. In this research, crystal structures of Alicyclobacillus acidocaldarius protein formerly annotated as an ACAD were determined in Apo and FAD bound state. Although our structure showed high structural similarity to other ACADs, close comparison of substrate binding pocket and phylogenetic analysis showed that this protein is more closely related to other bacterial group D flavin dependent monooxygenases, such as DszC (sulfoxidase) and DnmZ and Kijd3 (nitrososynthases).

Original languageEnglish
Article number548
Issue number11
StatePublished - Nov 2019


  • Acyl-CoA dehydrogenase
  • FAD
  • Flavin dependent monooxygenase


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