Abstract
Inhibition of recombinant D-amino acid oxidase from Trigonopsis variabilis (TvDAAO) activity in the presence of different sodium salts and potassium chloride is reported. A competitive inhibition pattern by sodium chloride was observed, and an inhibition constant value of Ki = 85 mM was calculated. Direct connection of NaCl inhibition with FAD cofactor dissociation was confirmed by measuring the fluorescence of tryptophanyl residues of the holoenzyme. Copyright © 2011 Jessica Kopf et al.
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CITATION STYLE
Kopf, J., Hormigo, D., García, J. L., Acebal, C., De La Mata, I., & Arroyo, M. (2011). Inhibition of recombinant D-amino acid oxidase from trigonopsis variabilis by salts. Enzyme Research, 2011(1). https://doi.org/10.4061/2011/158541
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