Inhibition of Recombinant D-Amino Acid Oxidase from Trigonopsis variabilis by Salts

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 K(i) = 85 mM was calculated...

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Detalles Bibliográficos
Autores principales: Kopf, Jessica, Hormigo, Daniel, García, José Luis, Acebal, Carmen, de la Mata, Isabel, Arroyo, Miguel
Formato: Texto
Lenguaje:English
Publicado: SAGE-Hindawi Access to Research 2011
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3057018/
https://www.ncbi.nlm.nih.gov/pubmed/21423676
http://dx.doi.org/10.4061/2011/158541
Descripción
Sumario: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 K(i) = 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.

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