title: Enzyme assay for pyridoxal 5'-phosphate by apo-D-amino acid aminotransferase.
abstract: D-amino acid aminotransferase (D-AAT) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme. D-AAT from thermophilic Bacillus sp. YM-1 was inactivated by ultraviolet irradiation. The activity was restored by the addition of PLP and showed a linear correlation with respect to PLP concentrations in the range of 10-40 nM.
authors.affiliation: Department of Applied Molecular Chemistry, College of Industrial Technology, Nihon University, 1-2-1 Izumichou, Narashino, Chiba 275-8575, Japan.
authors.forename: Hiroki
authors.initials: H
authors.lastname: Ota
authors.affiliation: Department of Applied Molecular Chemistry, College of Industrial Technology, Nihon University, 1-2-1 Izumichou, Narashino, Chiba 275-8575, Japan.
authors.forename: Masuwo
authors.initials: M
authors.lastname: Mushiga
authors.affiliation: Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.
authors.forename: Tohru
authors.initials: T
authors.lastname: Yoshimura
authors.affiliation: Department of Applied Molecular Chemistry, College of Industrial Technology, Nihon University, 1-2-1 Izumichou, Narashino, Chiba 275-8575, Japan. Electronic address: yoshimune.kazuaki@nihon-u.ac.jp.
authors.forename: Kazuaki
authors.initials: K
authors.lastname: Yoshimune
mesh_terms: D000596:Amino Acids / Q000378:metabolism*; D001051:Apoenzymes / Q000378:metabolism; D001407:Bacillus / Q000201:enzymology*; D057075:Enzyme Assays / Q000379:methods*; D011732:Pyridoxal Phosphate / Q000378:metabolism* / Q000494:pharmacology; D000637:Transaminases / Q000378:metabolism* / Q000528:radiation effects
chemical_list: D000596:Amino Acids; D001051:Apoenzymes; D011732:Pyridoxal Phosphate; D000637:Transaminases
keywords: Apoenzyme; Enzyme assay; Pyridoxal 5′-phosphate; Ultraviolet irradiation; d-Amino acid aminotransferase