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
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author Kopf, Jessica
Hormigo, Daniel
García, José Luis
Acebal, Carmen
de la Mata, Isabel
Arroyo, Miguel
author_facet Kopf, Jessica
Hormigo, Daniel
García, José Luis
Acebal, Carmen
de la Mata, Isabel
Arroyo, Miguel
author_sort Kopf, Jessica
collection PubMed
description 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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spelling pubmed-30570182011-03-21 Inhibition of Recombinant D-Amino Acid Oxidase from Trigonopsis variabilis by Salts Kopf, Jessica Hormigo, Daniel García, José Luis Acebal, Carmen de la Mata, Isabel Arroyo, Miguel Enzyme Res Research Article 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. SAGE-Hindawi Access to Research 2011-03-02 /pmc/articles/PMC3057018/ /pubmed/21423676 http://dx.doi.org/10.4061/2011/158541 Text en Copyright © 2011 Jessica Kopf et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Kopf, Jessica
Hormigo, Daniel
García, José Luis
Acebal, Carmen
de la Mata, Isabel
Arroyo, Miguel
Inhibition of Recombinant D-Amino Acid Oxidase from Trigonopsis variabilis by Salts
title Inhibition of Recombinant D-Amino Acid Oxidase from Trigonopsis variabilis by Salts
title_full Inhibition of Recombinant D-Amino Acid Oxidase from Trigonopsis variabilis by Salts
title_fullStr Inhibition of Recombinant D-Amino Acid Oxidase from Trigonopsis variabilis by Salts
title_full_unstemmed Inhibition of Recombinant D-Amino Acid Oxidase from Trigonopsis variabilis by Salts
title_short Inhibition of Recombinant D-Amino Acid Oxidase from Trigonopsis variabilis by Salts
title_sort inhibition of recombinant d-amino acid oxidase from trigonopsis variabilis by salts
topic Research Article
url 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
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