Mechanisms in Bioenergetics by Efraim Racker, Anthony San Pietro

By Efraim Racker, Anthony San Pietro

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Carbon dioxide is liberated in the first step. The second step consists of an oxidation of the succinic semialdehyde thiamine pyrophosphate intermediate by enzyme-bound lipoate, resulting in the formation of succinyl lipoate. Thiamine pyrophosphate becomes available again for another cycle of decarboxylation. As mentioned previously, the mechanism of this oxidation has been visualized as similar to the mechanism of glyceraldehyde 3-phosphate oxidation, except that the hydrogen acceptor is a sulfur of lipoate rather than carbon 4 of DPN.

The third type is in competition with biosynthesis. It 33 Oxidation of Glyceraldehyde 8-Phosphate will be discussed in detail under control mechanisms of energy metabolism. 4. The enzyme catalyzes the hydrolysis of acetyl phosphate. Like phosphate transfer, this reaction is also dependent on DPN. It is relatively slow with native enzyme, but much more rapid in aged preparations that have become "oxidized," as was first shown by Harting. 24 Treatment of the enzyme with oxidizing agents such as H2O2 accelerates its hydrolytic activity.

Since imidazole is known to serve as an acyl transfer agent in a nonenzymic reaction, as well as in some enzyme-catalyzed reactions in bacteria, this finding may represent an important clue to the mechanism of the reaction. LECTURE 5 PHOSPHOROCLASTIC REACTIONS: PHOSPHOKETOLASE Rather I prize the doubt Low kinds exist without, Finished and finite clods, untroubled by a spark. —Robert Browning, "Rabbi ben Ezra" The reactions of the second group, which lead to ATP formation via a phosphoroclastic cleavage of a carbon-carbon, a carbon-nitrogen, or a carbon-sulfur bond, are found primarily among microorganisms.

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