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The reaction it catalyzes is: pyruvate + HCO − 3 + ATP → oxaloacetate + ADP + P. It is an important anaplerotic reaction that creates oxaloacetate from pyruvate. PC contains a biotin prosthetic group [1] and is typically localized to the mitochondria in eukaryotes with exceptions to some fungal species such as Aspergillus nidulans which have a cytosolic PC.
Now this pyruvate can easily enter the mitochondria, where it is carboxylated again to oxaloacetate by pyruvate carboxylase. In this way, the transfer of acetyl-CoA that is from the mitochondria into the cytoplasm produces a molecule of NADH. The overall reaction, which is spontaneous, may be summarized as:
1) Carbon is fixed to produce oxaloacetate by PEP carboxylase. 2) The four carbon molecule then exits the cell and enters the chloroplasts of bundle sheath cells. 3) It is then broken down releasing carbon dioxide and producing pyruvate. Carbon dioxide combines with ribulose bisphosphate and proceeds to the Calvin Cycle.
Pyruvate generated from alanine will enter glyceroneogenesis and generate glycerol 3-phosphate. Glutamate can also enter glyceroneogenesis. Since the key reaction of glyceroneogenesis is the decarboxylation and phosphorylation of oxaloacetate to phosphoenolpyruvate, in theory any biochemical pathway which generates oxaloacetate is related to ...
Pyruvate + 2 H + + 2 e − → Lactate-0.19 [9] Oxaloacetate + 2 H + + 2 e − → Malate-0.17 [10] While under standard conditions malate cannot reduce the more electronegative NAD +:NADH couple, in the cell the concentration of oxaloacetate is kept low enough that Malate dehydrogenase can reduce NAD + to NADH during the citric acid cycle.
Pyruvate molecules produced by glycolysis are actively transported across the inner mitochondrial membrane, and into the matrix where they can either be oxidized and combined with coenzyme A to form CO 2, acetyl-CoA, and NADH, [35] or they can be carboxylated (by pyruvate carboxylase) to form oxaloacetate. This latter reaction "fills up" the ...
Oxaloacetate decarboxylase is a carboxy-lyase involved in the conversion of oxaloacetate into pyruvate.. It is categorized under EC 4.1.1.3.. Oxaloacetate decarboxylase activity in a given organism may be due to activity of malic enzyme, pyruvate kinase, malate dehydrogenase, pyruvate carboxylase and PEP carboxykinase or the activity of "real" oxaloacetate decarboxylases.
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]