Limited proteolysis and X-ray crystallography reveal the origin of substrate specificity and of the rate-limiting product release during oxidation of D-amino acids catalyzed by mammalian D-amino acid oxidase.
Vanoni MA, Cosma A, Mazzeo D, Mattevi A, Todone F, Curti B.
Vanoni MA, et al. Among authors: mattevi a.
Biochemistry. 1997 May 13;36(19):5624-32. doi: 10.1021/bi963023s.
Biochemistry. 1997.
PMID: 9153402
Limited proteolysis of D-amino acid oxidase holoenzyme with trypsin cleaves the protein at Arg 221 and near the C-terminus, producing stable 25, 13.4, and 2 kDa polypeptides [Torri-Tarelli, G., Vanoni, M. A., Negri, A., & Curti, B. (1990) J. Biol. Chem. 265, 212 …
Limited proteolysis of D-amino acid oxidase holoenzyme with trypsin cleaves the protein at Arg 221 and near the C-terminus, producing stable …