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Pyruvate carboxylase (PC) encoded by the gene PC is an enzyme (EC 6.4.1.1) of the ligase class that catalyzes (depending on the species) the physiologically irreversible [citation needed] carboxylation of pyruvate to form oxaloacetate (OAA).
Oxaloacetic acid (also known as oxalacetic acid or OAA) is a crystalline organic compound with the chemical formula HO 2 CC(O)CH 2 CO 2 H. Oxaloacetic acid, in the form of its conjugate base oxaloacetate, is a metabolic intermediate in many processes that occur in animals.
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 ]
Pyruvate dehydrogenase complex. Pyruvate dehydrogenase complex (PDC) is a complex of three enzymes that converts pyruvate into acetyl-CoA by a process called pyruvate decarboxylation. [1] Acetyl-CoA may then be used in the citric acid cycle to carry out cellular respiration, and this complex links the glycolysis metabolic pathway to the citric ...
When pyruvate kinase – the enzyme that normally catalyzes the reaction that converts PEP to pyruvate – is knocked out in mutants of Bacillus subtilis, PEPCK participates in one of the replacement anaplerotic reactions, working in the reverse direction of its normal function, converting PEP to OAA. [13]
Pyruvate carboxylase deficiency is an inherited disorder that causes lactic acid to accumulate in the blood. [2] High levels of these substances can damage the body's organs and tissues, particularly in the nervous system. Pyruvate carboxylase deficiency is a rare condition, with an estimated incidence of 1 in 250,000 births worldwide.
In enzymology, formate C-acetyltransferase (pyruvate formate lyase) (EC 2.3.1.54) is an enzyme. Pyruvate formate lyase is found in Escherichia coli [1] and other organisms. It helps regulate anaerobic glucose metabolism. Using radical non-redox chemistry, it catalyzes the reversible conversion of pyruvate and coenzyme-A into formate and acetyl ...
Here, the OAA produced by PEPC is transaminated by aspartate aminotransferase to aspartate (ASP) which is the metabolite diffusing to the bundle sheath. In the bundle sheath ASP is transaminated again to OAA and then undergoes a futile reduction and oxidative decarboxylation to release CO 2. The resulting Pyruvate is transaminated to alanine ...