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Polycarboxylic acid synthases

Polycarboxylic acid synthases. Several enzymes, including citrate synthase, the key enzyme which catalyzes the first step of the citric acid cycle, promote condensations of acetyl-CoA with ketones (Eq. 13-38). An a-oxo acid is most often the second substrate, and a thioester intermediate (Eq. 13-38) undergoes hydrolysis to release coenzyme A.199 Because the substrate acetyl-CoA is a thioester, the reaction is often described as a Claisen condensation. The same enzyme that catalyzes the condensation of acetyl-CoA with a ketone also catalyzes the second step, the hydrolysis of the CoA thioester. These polycarboxylic acid synthases are important in biosynthesis. They carry out the initial steps in a general chain elongation process (Fig. 17-18). While one function of the thioester group in acetyl-CoA is to activate the methyl hydrogens toward the aldol condensation, the subsequent hydrolysis of the thioester linkage provides for overall irreversibility and "drives" the synthetic reaction. [Pg.700]

Polycarboxylate synthases, table 700 Poly carboxylic acid synthases 700 - 703 Polyethylene... [Pg.929]


See other pages where Polycarboxylic acid synthases is mentioned: [Pg.676]    [Pg.676]    [Pg.700]    [Pg.676]    [Pg.676]    [Pg.700]    [Pg.276]   
See also in sourсe #XX -- [ Pg.700 , Pg.701 , Pg.702 ]

See also in sourсe #XX -- [ Pg.700 , Pg.701 , Pg.702 ]

See also in sourсe #XX -- [ Pg.700 , Pg.701 , Pg.702 ]




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