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1. CO 2 is fixed to produce a four-carbon molecule (malate or aspartate). 2. The molecule exits the cell and enters the bundle sheath cells. 3. It is then broken down into CO 2 and pyruvate. CO 2 enters the Calvin cycle to produce carbohydrates. 4. Pyruvate reenters the mesophyll cell, where it is reused to produce malate or aspartate.
The reaction is similar to the reaction catalysed by pyruvate kinase, which also converts pyruvate to PEP. [3] However, pyruvate kinase catalyses an irreversible reaction, and does not consume ATP. By contrast, PPDK catalyses a reversible reaction, and consumes 1 molecule of ATP for each molecule of pyruvate converted.
Pyruvate, the conjugate base, CH 3 COCOO −, is an intermediate in several metabolic pathways throughout the cell. Pyruvic acid can be made from glucose through glycolysis , converted back to carbohydrates (such as glucose) via gluconeogenesis , or converted to fatty acids through a reaction with acetyl-CoA . [ 3 ]
The pyruvate produced by glycolysis is an important intermediary in the conversion of carbohydrates into fatty acids and cholesterol. [46] This occurs via the conversion of pyruvate into acetyl-CoA in the mitochondrion. However, this acetyl CoA needs to be transported into cytosol where the synthesis of fatty acids and cholesterol occurs.
Pyruvate is oxidized to acetyl-CoA and CO 2 by the pyruvate dehydrogenase complex (PDC). The PDC contains multiple copies of three enzymes and is located in the mitochondria of eukaryotic cells and in the cytosol of prokaryotes. In the conversion of pyruvate to acetyl-CoA, one molecule of NADH and one molecule of CO 2 is formed. [11]
Pyruvate oxidation is the step that connects glycolysis and the Krebs cycle. [4] In glycolysis, a single glucose molecule (6 carbons) is split into 2 pyruvates (3 carbons each). Because of this, the link reaction occurs twice for each glucose molecule to produce a total of 2 acetyl-CoA molecules, which can then enter the Krebs cycle.
Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle.All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester) as a substrate.
Phosphoenolpyruvate carboxylase (also known as PEP carboxylase, PEPCase, or PEPC; EC 4.1.1.31, PDB ID: 3ZGE) is an enzyme in the family of carboxy-lyases found in plants and some bacteria that catalyzes the addition of bicarbonate (HCO 3 −) to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate: [1]