Enzyme assay for pyridoxal 5'-phosphate by apo-D-amino acid aminotransferase

Hiroki Ota; Masuwo Mushiga; Tohru Yoshimura; Kazuaki Yoshimune

doi:10.1016/j.jbiosc.2014.12.006

Enzyme assay for pyridoxal 5'-phosphate by apo-D-amino acid aminotransferase

J Biosci Bioeng. 2015 Jul;120(1):117-9. doi: 10.1016/j.jbiosc.2014.12.006. Epub 2015 Jan 24.

Authors

Hiroki Ota¹, Masuwo Mushiga¹, Tohru Yoshimura², Kazuaki Yoshimune³

Affiliations

¹ Department of Applied Molecular Chemistry, College of Industrial Technology, Nihon University, 1-2-1 Izumichou, Narashino, Chiba 275-8575, Japan.
² Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.
³ 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.

PMID: 25622769
DOI: 10.1016/j.jbiosc.2014.12.006

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.

Keywords: Apoenzyme; Enzyme assay; Pyridoxal 5′-phosphate; Ultraviolet irradiation; d-Amino acid aminotransferase.

MeSH terms

Amino Acids / metabolism*
Apoenzymes / metabolism
Bacillus / enzymology*
Enzyme Assays / methods*
Pyridoxal Phosphate / metabolism*
Pyridoxal Phosphate / pharmacology
Transaminases / metabolism*
Transaminases / radiation effects

Substances

Amino Acids
Apoenzymes
Pyridoxal Phosphate
Transaminases