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Inhibition of Recombinant D-Amino Acid Oxidase fromTrigonopsis variabilisby Salts
Author(s) -
Jessica Kopf,
Daniel Hormigo,
José L. Garcı́a,
Carmen Acebal,
Isabel de la Mata,
Miguel Arroyo
Publication year - 2011
Publication title -
enzyme research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.439
H-Index - 39
eISSN - 2090-0406
pISSN - 2090-0414
DOI - 10.4061/2011/158541
Subject(s) - d amino acid oxidase , recombinant dna , amino acid , chemistry , oxidase test , biochemistry , cancer research , enzyme , medicine , gene
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

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