Abstract
Porcine kidney betaine aldehyde dehydrogenase (EC 1.2.1.8) kinetic properties were determined at low substrate concentrations. The double-reciprocal plots of initial velocity versus substrate concentration are linear and intersect at the left of the 1/v axis and showed substrate inhibition with betaine aldehyde. Studies of inhibition by NADH and dead-end analogs showed that NADH is a mixed inhibitor against NAD+ and betaine aldehyde. AMP is competitive with respect to NAD+ and mixed with betaine aldehyde. Choline is competitive against betaine aldehyde and uncompetitive with respect to NAD+. The kinetic behavior is consistent with an Iso-Ordered Bi-Bi Steady-State mechanism.
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