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Table 2.
Effects of cofactors and inhibitors on IDO activity.
Additive in reaction mixtureHIL produced (mM)
–0.00
α-KG0.00
Ascorbic acid0.00
Fe2+0.00
α-KG, ascorbic acid0.00
α-KG, Fe2+0.02
α-KG, ascorbic acid, Fe2+0.26
α-KG, ascorbic acid, Fe2+, EDTA0.00
α-KG, ascorbic acid, Fe2+, ZnCl20.00
α-KG, ascorbic acid, Fe2+, CuCl20.00
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The effect of SCH900776 on IDO activity was assayed under standard conditions, except that the reaction pH was varied between 2.0 and 12.0. The maximum activity of 4-HIL formation was detected at pH 6.0. In addition, the effect of temperature on IDO activity was assayed under the standard conditions, except that the reaction temperature was changed between °C and 70 °C. The maximum reaction rate of IDO was detected at 30 °C.
Structure analysis of 4-HIL produced from l-Ile by IDO
4-HIL produced by the purified enzyme was isolated and subjected to structural analysis. As shown in Fig. 3, the NMR spectrum of the enzymatically prepared HIL was the same as that of HIL extracted from fenugreek seeds; confirming that the hydroxylation site is the C4-position of l-Ile.