Characterization of the inhibition effect induced by nickel on glucose-6-phosphate dehydrogenase and glutathione reductase.
Kinetic characterization of the inhibition effect of nickel on glucose-6-phosphate dehydrogenase (EC 1.1.1.49) (G-6-PD) and glutathione reductase (GR; EC 1.6.4.2) from Saccharomyces cerevisiae was made. The effect of nickel on G-6-PD activity is consistent with a mixed-type inhibition pattern, with a competitive character, since the inequality ki,int greater than ki,slope shows an inverse relation between varied substrate concentrations and fractional inhibition. An inhibition effect of nickel on GR activity, when NADPH is the varied substrate, is also consistent with a mixed-type inhibition pattern. However, pure competitive inhibition is found on GR reaction when oxidized glutathione is the varied substrate. This investigation shows the highest sensibility of GR before the inhibitory effect of nickel, in agreement with the experimental values of inhibition constants found in this study, where constants related to the GR system are lower than the ones of the G-6-PD system.[1]References
- Characterization of the inhibition effect induced by nickel on glucose-6-phosphate dehydrogenase and glutathione reductase. Cartañá, J., Arola, L., Romeu, A. Enzyme (1989) [Pubmed]
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