Pre-Steady State Kinetics of the NAD-Malic Enzyme from Ascaris suum in the Direction of Oxidative Decarboxylation of L-Malate

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Stopped-flow experiments in which the NAD-malic enzyme was preincubated with different reactants at near saturating substrate concentrations suggest a slow isomerization of the E:NAD:Mg complex. The lag is eliminated by preincubation with Mg˙² and malate suggesting that the formation of E:Mg:Malate either bypasses or speeds up the slow isomerization step. Circular dichroic spectral studies of the secondary structural changes of the native enzyme in the presence and absence of substrates supports the existence of conformational changes with NAD˙ and malate. Thus, a slow conformational change of the E:NAD:Mg complex is likely one of the rate-limiting steps in the pre-steady state.

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vii, 67 leaves: ill.

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Rajapaksa, Ranjani, 1949- December 1991.

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  • Rajapaksa, Ranjani, 1949-

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Stopped-flow experiments in which the NAD-malic enzyme was preincubated with different reactants at near saturating substrate concentrations suggest a slow isomerization of the E:NAD:Mg complex. The lag is eliminated by preincubation with Mg˙² and malate suggesting that the formation of E:Mg:Malate either bypasses or speeds up the slow isomerization step. Circular dichroic spectral studies of the secondary structural changes of the native enzyme in the presence and absence of substrates supports the existence of conformational changes with NAD˙ and malate. Thus, a slow conformational change of the E:NAD:Mg complex is likely one of the rate-limiting steps in the pre-steady state.

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vii, 67 leaves: ill.

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  • December 1991

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  • March 9, 2015, 8:15 a.m.

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  • Sept. 13, 2017, 12:26 p.m.

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Rajapaksa, Ranjani, 1949-. Pre-Steady State Kinetics of the NAD-Malic Enzyme from Ascaris suum in the Direction of Oxidative Decarboxylation of L-Malate, thesis, December 1991; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc500668/: accessed November 22, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .