Chiaki Setoyama

TL;DR: The X-ray crystallographic structure of porcine kidney D-amino acid oxidase, which had been expressed in Escherichia coli transformed with a vector containing DAO cDNA, was determined by the isomorphous replacement method for the complex form with benzoate.

TL;DR: It is demonstrated that mtDNA-like sequences are present in human nuclear DNA.

TL;DR: Comparison of the amino acid sequences among the mammalian and bacterial MDHs revealed that the homology between the mouse cMDH and thermophilic bacterialMDH, as well as the homological between the mice mMDHand Escherichia coli MDH markedly exceeds the intraspecies sequence homology.

TL;DR: The X-ray analysis showed that the overall folding of ACO-II less C-terminal 221 residues is similar to that of medium-chain acyl-CoA dehydrogenase (MCAD), suggesting that the C-Terminal domain moves to close the active site upon substrate binding.

TL;DR: This model enables the evaluation of the substrate-flavin interaction prior to electron transfer from the substrate to flavin and provides two possible mechanisms for the reductive-half reaction of DAO, i.e., the electron-proton-electron transfer mechanism and the ionic mechanism.