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Pyruvate-carboxylase

Pyruvate carboxylase is another enzyme which is not a part of the citric acid cycle per se but which functions in close association with it. The function of this enzyme is described in Chap. 11. but it is useful to consider its action, and that of pyruvate dehydrogenase, in relation to the citric acid cycle. [Pg.353]

The product of this reaction, oxaloacetate, can either enter the gluconeogenic pathway (Chap. 11) by way of malate or condense with acetyl-CoA to yield citrate. Pyruvate carboxylase is an allosteric enzyme, and it is activated by the heterotropic effector, acetyl-CoA. Thus, pyruvate in the mitochondria is the substrate for either pyruvate dehydrogenase or pyruvate carboxylase, the activities of which, in turn, are controlled by reactants associated with the citric acid cycle. The interplay among pyruvate dehydrogenase, pyruvate carboxylase, pyruvate, and the citric acid cycle is shown in Fig. 12-9. [Pg.353]

2 Pyruvate Carboxylase Pyruvate carboxylase catalyzes the car-boxylation of pyruvate to oxaloacetate - both the first committed step of gluconeogenesis from pyruvate and also an important anaplerotic reaction, permitting repletion of tricarboxylic acid cycle intermediates and hence fatty acid synthesis. The mammalian enzyme is activated aUosterically by acetyl CoA, which accumulates when there is a need for increased activity of pyruvate carboxylase to synthesize oxaloacetate to permit increased citric acid cycle activity or for gluconeogenesis (Attwood, 1995 Jitrapakdee and Wallace, 1999). [Pg.331]

Pyruvate carboxylase is also important in lipogenesis. Citrate is transported out of mitochondria and cleaved in the cytosol to provide acetyl CoA for fatty acid synthesis the resultant oxaloacetate is reduced to malate, which undergoes oxidative decarboxylation to pyruvate, a reaction that provides at least half of the NADPH required for fatty acid synthesis. Pyruvate reenters the mitochondria and is carboxylated to oxaloacetate to maintain the process. [Pg.331]

Mammalian pyruvate carboxylase has four identical subunits, and the isolated monomer will catalyze the complete reaction. By contrast, three distinct subunits can be isolated from acetyl CoA carboxylase of Escherichia coli and spinach chloroplasts a biotinyl carrier protein, biotin carboxylase, and carboxyl transferase. [Pg.331]

Genetic deficiency of pyruvate carboxylase does not cause the expected hypoglycemia. Rather, it seems that depletion of tissue pools of oxaloacetate results in impaired activity of citrate synthase, and a slowing of citric acid cycle activity, leading to accumulation of lactate, pyruvate, and alanine, and also increased accumulation of acetyl CoA, resulting in ketosis. Affected infants have serious neurological problems and rarely survive. A less severe variant of the disease is associated with low residual activity of pyruvate carboxylase. [Pg.331]


In a sort of reciprocal arrangement, the cell also feeds many intermediates back into the TCA cycle from other reactions. Since such reactions replenish the TCA cycle intermediates, Hans Kornberg proposed that they be called anaplerotie reactions (literally, the filling up reactions). Thus, PEP carboxylase and pyruvate carboxylase synthesize oxaloacetate from pyruvate (Figure 20.24). [Pg.663]

Pyruvate carboxylase is the most important of the anaplerotie reactions. It exists in the mitochondria of animal cells but not in plants, and it provides a direct link between glycolysis and the TCA cycle. The enzyme is tetrameric and contains covalently bound biotin and an Mg site on each subunit. (It is examined in greater detail in our discussion of gluconeogenesis in Chapter 23.) Pyruvate carboxylase has an absolute allosteric requirement for acetyl-CoA. Thus, when acetyl-CoA levels exceed the oxaloacetate supply, allosteric activation of pyruvate carboxylase by acetyl-CoA raises oxaloacetate levels, so that the excess acetyl-CoA can enter the TCA cycle. [Pg.663]

Two particularly interesting aspects of the pyruvate carboxylase reaction are (a) allosteric activation of the enzyme by acyl-coenzyme A derivatives and (b) compartmentation of the reaction in the mitochondrial matrix. The carboxy-lation of biotin requires the presence (at an allosteric site) of acetyl-coenzyme A or other acylated coenzyme A derivatives. The second half of the carboxylase reaction—the attack by pyruvate to form oxaloacetate—is not affected by CoA derivatives. [Pg.745]

FIGURE 23.4 A mechanism for the pyruvate carboxylase reaction. Bicarbonate must be activated for attack by the pyruvate carbanion. This activation is driven by ATP and involves formation of a carbonylphosphate intermediate —a mixed anhydride of carbonic and phosphoric acids. (Carbonylphosphate and car-boxyphosphate are synonyms.)... [Pg.746]

COMPARTMENTALIZED PYRUVATE CARBOXYLASE DEPENDS ON METABOLITE CONVERSION AND TRANSPORT The second interesting feature of pyruvate carboxylase is that it is found only in the matrix of the mitochondria. By contrast, the next enzyme in the gluconeogenic pathway, PEP carboxykinase, may be localized in the cytosol or in the mitochondria or both. For example, rabbit liver PEP carboxykinase is predominantly mitochondrial, whereas the rat liver enzyme is strictly cytosolic. In human liver, PEP carboxykinase is found both in the cytosol and in the mitochondria. Pyruvate is transported into the mitochondrial matrix, where it can be converted to acetyl-CoA (for use in the TCA cycle) and then to citrate (for fatty acid synthesis see Figure 25.1). /Uternatively, it may be converted directly to 0/ A by pyruvate carboxylase and used in glu-... [Pg.746]

Acetyl-CoA is a potent allosteric effector of glycolysis and gluconeogenesis. It allosterically inhibits pyruvate kinase (as noted in Chapter 19) and activates pyruvate carboxylase. Because it also allosterically inhibits pyruvate dehydrogenase (the enzymatic link between glycolysis and the TCA cycle), the cellular fate of pyruvate is strongly dependent on acetyl-CoA levels. A rise in... [Pg.750]

Based on the mechanism for pyruvate carboxylase (Figure 23.4), write reasonable mechanisms for the reactions shown below ... [Pg.773]

Step 1 of Figure 29.13 Carboxylation Gluconeogenesis begins with the carboxyl-afion of pyruvate to yield oxaloacetate. The reaction is catalyzed by pyruvate carboxylase and requires ATP, bicarbonate ion, and the coenzyme biotin, which acts as a carrier to transport CO2 to the enzyme active site. The mechanism is analogous to that of step 3 in fatty-acid biosynthesis (Figure 29.6), in which acetyl CoA is carboxylated to yield malonyl CoA. [Pg.1162]

Biotin is involved in carboxylation and decarboxylation reactions. It is covalently bound to its enzyme. In the carboxylase reaction, C02 is first attached to biotin at the ureido nitrogen, opposite the side chain in an ATP-dependent reaction. The activated C02 is then transferred from carboxybiotin to the substrate. The four enzymes of the intermediary metabolism requiring biotin as a prosthetic group are pyruvate carboxylase (pyruvate oxaloacetate), propionyl-CoA-carboxylase (propionyl-CoA methylmalonyl-CoA), 3-methylcroto-nyl-CoA-carboxylase (metabolism of leucine), and actyl-CoA-carboxylase (acetyl-CoA malonyl-CoA) [1]. [Pg.270]

Pyruvic acid is an intermediate in the fermentation of grains. During fermentation the enzyme pyruvate carboxylase causes the pyruvate ion to release carbon dioxide. In one experiment a 200.-mL aqueous solution of the pyruvate in a sealed, rigid 500.-mL flask at 293 K had an initial concentration of 3.23 mmol-L -l. Because the concentration of the enzyme was kept constant, the reaction was pseudo-first order in pyruvate ion. The elimination of CU2 by the reaction was monitored by measuring the partial pressure of the C02 gas. The pressure of the gas was found to rise from zero to 100. Pa in 522 s. What is the rate constant of the pseudo-first order reaction ... [Pg.693]

An intriguing stress-induced alteration in gene expression occurs in a succulent plant, Mesembryanthemum crystallinum, which switches its primary photosynthetic CO2 fixation pathway from C3 type to CAM (Crassulacean acid metabolism) type upon salt or drought stress (Winter, 1974 Chapter 8). Ostrem et al. (1987) have shown that the pathway switching involves an increase in the level of mRNA encoding phosphoenol-pyruvate carboxylase, a key enzyme in CAM photosynthesis. [Pg.165]

Mitochondrial pyruvate carboxylase catalyzes the cat-boxylation of pymvate to oxaloacetate, an ATP-tequit-ing reaction in which the vitamin biotin is the coenzyme. Biotin binds CO2 from bicatbonate as carboxybiotin ptiot to the addition of the COj to pym-... [Pg.153]

Enzymes of gluconeogc Pyruvate carboxylase mesis t Glucocorticoids, glucagon, epinephrine (cAMP) Insulin Acetyl-CoA ADP ... [Pg.156]

Theoretically, a fall in concentration of oxaloacetate, particularly within the mitochondria, could impair the ability of the citric acid cycle to metabolize acetyl-CoA and divert fatty acid oxidation toward ketogenesis. Such a fall may occur because of an increase in the [NADH]/[NAD+] ratio caused by increased P-oxida-tion affecting the equilibrium between oxaloacetate and malate and decreasing the concentration of oxaloacetate. However, pyruvate carboxylase, which catalyzes the conversion of pyruvate to oxaloacetate, is activated by acetyl-CoA. Consequently, when there are significant amounts of acetyl-CoA, there should be sufficient oxaloacetate to initiate the condensing reaction of the citric acid cycle. [Pg.187]

J. F. Johnson, C. P. Vance, and D. L. Allan, Phosphorus deficiency in Lupinus aUms altered lateral root development and enhanced expression of phosphoenol-pyruvate carboxylase. Plant Physiol. 112 31 (1996). [Pg.83]

The Jirst indirect route in glucose synthesis involves the formation of phosphoenolpyruvate from pyruvate without the intervention of pyruvate kinase. This route is catalyzed by two enzymes. At first, pyruvate is converted into oxaloacetate. This reaction occurs in the mitochondria as the pyruvate molecules enter them, and is catalyzed by pyruvate carboxylase according to the scheme... [Pg.186]

The free glucose produced by this reaction is supplied to the blood from the tissues. As exemplified by gluconeogenesis, one may easily envision the economical organization of these metabolic routes, since, apart from four special gluconeogenesis enzymes-pyruvate carboxylase, phosphopyruvate carboxylase, fructose bisphosphatase, and glucose 6-phosphatase-individual glycolytic enzymes are also used in the gluconeogenesis. [Pg.187]

The reactions that convert pyruvate to intermediates of the TCA cycle are called the anaplerotic reactions. Pyruvate, which can be made only from glucose or some of the amino acids, can be converted to oxaloacetate by the enzyme pyruvate carboxylase or to malate by malic enzyme. [Pg.206]


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Biotin pyruvate carboxylase

Carboxylase

Carboxylases

Citrate cycle Pyruvate carboxylase

Citric acid cycle pyruvate carboxylase

Enzyme pyruvate carboxylase

Enzymes phosphoenol pyruvate carboxylase

Gluconeogenesis Pyruvic carboxylase

Gluconeogenesis pyruvate carboxylase activation

Gluconeogenesis, biotin pyruvate carboxylase

Glycolysis Pyruvic carboxylase

Mitochondria pyruvate carboxylase

Oxaloacetate pyruvate carboxylase deficiency

Phosphoenol-pyruvate carboxylase

Phosphoenolpyruvate carboxylase, pyruvate

Phosphoenolpyruvate carboxylase, pyruvate decarboxylation

Pyruvate carboxylase (PYC

Pyruvate carboxylase biotin dependent

Pyruvate carboxylase biotin metabolism

Pyruvate carboxylase catalyses

Pyruvate carboxylase control mechanisms

Pyruvate carboxylase deficiency

Pyruvate carboxylase first partial reaction

Pyruvate carboxylase gluconeogenesis

Pyruvate carboxylase lipoic acid

Pyruvate carboxylase model

Pyruvate carboxylase modification

Pyruvate carboxylase modifiers

Pyruvate carboxylase partial reactions

Pyruvate carboxylase reaction catalyzed

Pyruvate carboxylase regulation

Pyruvate carboxylase requirements

Pyruvate carboxylase stimulation

Pyruvate carboxylase structure

Pyruvate carboxylase substrate cycle

Pyruvate carboxylase temperature

Pyruvate carboxylase, activity

Pyruvate carboxylase, function

Pyruvate carboxylases and

Pyruvic carboxylase

Thiamine pyruvate with carboxylase

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