Inhibition of Recombinant D-Amino Acid Oxidase from Trigonopsis variabilis by Salts
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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.
Evidence for the functional importance of Cys298 in D-amino acid oxidase from Trigonopsis variabilis
1993 ◽
Vol 218
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pp. 735-744
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2000 ◽
Vol 186
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pp. 215-219
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2001 ◽
Vol 95
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pp. 083-092
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1985 ◽
Vol 31
(7)
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pp. 625-628
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2010 ◽
Vol 1804
(7)
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pp. 1483-1491
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1962 ◽
Vol 27
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pp. 465-471
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