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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 …
Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis.
Bossi RT, Negri A, Tedeschi G, Mattevi A. Bossi RT, et al. Among authors: mattevi a. Biochemistry. 2002 Mar 5;41(9):3018-24. doi: 10.1021/bi015939r. Biochemistry. 2002. PMID: 11863440
L-Aspartate oxidase (Laspo) catalyzes the conversion of L-Asp to iminoaspartate, the first step in the de novo biosynthesis of NAD(+). This bacterial pathway represents a potential drug target since it is absent in mammals. The Laspo R386L mutant was crystallized in the FA …
L-Aspartate oxidase (Laspo) catalyzes the conversion of L-Asp to iminoaspartate, the first step in the de novo biosynthesis of NAD(+). This …
240 results