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

2011 ◽  
Vol 2011 ◽  
pp. 1-5
Author(s):  
Jessica Kopf ◽  
Daniel Hormigo ◽  
José Luis García ◽  
Carmen Acebal ◽  
Isabel de la Mata ◽  
...  

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.

1985 ◽  
Vol 31 (7) ◽  
pp. 625-628 ◽  
Author(s):  
Eva M. Kubicek-Pranz ◽  
M. Röhr

Production of D-amino-acid oxidase by Trigonopsis variabilis has been investigated using a two-stage cultivation technique. After transfer of exponentially growing cells to fresh medium, the enzyme was induced by addition of D-amino acids to the growth medium, among which D-methionine and D-alanine were the most effective. The simultaneous presence of the L form of amino acids or [Formula: see text] did not affect this induction. The presence of trace metals, inorganic phosphate, and a high rate of agitation were necessary for formation of maximal D-amino-acid oxidase activity. The enzyme is not subject to glucose repression.


1962 ◽  
Vol 27 (3) ◽  
pp. 465-471 ◽  
Author(s):  
S. Sentheshanmuganathan ◽  
W. J. Nickerson

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