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• W2161019938 abstract "Abstract Specific incorporation of [7-14C]nicotinamide into the malate-lactate transhydrogenase and the subsequent purification of the radioactive enzyme are reported. An amino acid composition of the purified enzyme is presented. The transhydrogenase does not appear to contain zinc since 65Zn cannot be incorporated into the protein. Furthermore, the enzyme activity is not inhibited by chelating agents. The native enzyme appears to have pyruvate bound tightly to the protein as measured by the incorporation of tritium from borotridide reduction and the subsequent isolation of [3H]lactate after protein hydrolysis. The role of this pyruvate in the mechanism is not known since reduction by borohydride causes only a 20% drop in enzymatic activity. Treatment of the transhydrogenase with NADase destroys enzymatic activity and releases nicotinic acid and nicotinamide from the enzyme. Treatment of the enzyme with 7 m urea, as well as 6 m guanidine-HCl and 0.1% sodium dodecyl sulfate causes a slow release of the whole prosthetic group, which has been isolated and identified as NAD-NADH. The apoenzyme which has been separated from the prosthetic group by gel filtration is virtually insoluble. Succinylation and 7 m urea can both be used to solubilize this protein which has been shown to have a molecular weight of approximately 30,000 x 106 by sucrose gradient centrifugation. The holoenzyme has a molecular weight of 100,000 to 115,000 x 106, and thus the enzyme appears to be composed of either three or four subunits. The kinetics of the transhydrogenation reaction yields results consistent with a type of ping-pong mechanism. The half-reactions have also been shown to proceed stoichiometrically. The over-all mechanism is more complex, however, as each product is a competitive inhibitor for the reaction and abortive complexes are formed. A mechanism based on the kinetic evidence and in agreement with that proposed by Dolin ((1969) J. Biol. Chem., 244, 5273) is presented." @default.
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• W2161019938 date "1972-02-01" @default.
• W2161019938 modified "2023-10-03" @default.
• W2161019938 title "Studies on the Structure and Mechanism of Action of the Malate-Lactate Transhydrogenase" @default.
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• W2161019938 doi "https://doi.org/10.1016/s0021-9258(19)45693-7" @default.
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