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- W2034647911 abstract "The kinetic mechanism of human liver aldehyde dehydrogenase, E1, was investigated at pH 7.2 using initial velocity, product inhibition, dead end inhibition, and pre-steady-state techniques. Only NADH, which was found to be competitive with NAD+ at high (mm) and low (μm) concentrations of acetaldehyde, could be used as a product inhibitor. Chloral hydrate was found to competitively inhibit the enzyme with respect to acetaldehyde and also produce a hyperbolic slope replot when NAD+ was varied. Adenosine 5′-monophosphate was competitive with NAD+ and noncompetitive with acetaldehyde as the varied substrate. The results indicate that the reaction mechanism proceeds mainly through an enzyme·NAD binary complex, but at high concentrations of aldehyde a small degree of randomness occurs. In order to gain information concerning the rate-limiting step, deuteroacetaldehyde was used and found to increase the Km of the aldehyde (KmCH3CDOCH3CHO=3) but have no effect on the steady-state maximal velocity. When enzyme·NAD was rapidly mixed with acetaldehyde in the stopped-flow apparatus, a “burst” of NADH was observed followed by a slower steady-state turnover, indicating that the rate-limiting step of the dehydrogenase reaction occurs after ternary complex interconversion. The magnitude of the “burst” using high specific activity E1 was that which would be expected for four active sites per tetramer, indicating all-of-the sites reactivity." @default.
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- W2034647911 date "1981-11-01" @default.
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- W2034647911 title "Kinetic mechanism of the human cytoplasmic aldehyde dehydrogenase E1" @default.
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- W2034647911 doi "https://doi.org/10.1016/0003-9861(81)90338-6" @default.
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