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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.
Pyruvate dehydrogenase complex reaction. Pyruvate decarboxylation or pyruvate oxidation, also known as the link reaction (or oxidative decarboxylation of pyruvate [1]), is the conversion of pyruvate into acetyl-CoA by the enzyme complex pyruvate dehydrogenase complex. [2] [3] The reaction may be simplified as:
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 ...
If the substrate bound in the active site is pyruvate, the enzyme is activated by a conformational change in this regulatory site. [6] The conformational change involves a 1,2 nucleophilic addition. This reaction, the formation of a thioketal, transforms the enzyme from its inactive to active state.
Pyruvate dehydrogenase is an enzyme that catalyzes the reaction of pyruvate and a lipoamide to give the acetylated dihydrolipoamide and carbon dioxide. The conversion requires the coenzyme thiamine pyrophosphate. Pyruvate dehydrogenase is usually encountered as a component, referred to as E1, of the pyruvate dehydrogenase complex (PDC). PDC ...
For simple decarboxylation reaction, the enzyme involved in this reaction is pyruvate decarboxylase, which is different from oxidative decarboxylation. During the reaction, pyruvate is directly connected with the thiazole ring of TPP, and the carboxyl group on pyruvate is removed after the connection to generate carbon dioxide.
During fasting state, pyruvate kinase is inhibited, thus preventing the "leak-down" of phosphoenolpyruvate from being converted into pyruvate; [17] instead, phosphoenolpyruvate is converted into glucose via a cascade of gluconeogenesis reactions. Although it utilizes similar enzymes, gluconeogenesis is not the reverse of glycolysis.
Pyruvate, phosphate dikinase, or PPDK (EC 2.7.9.1) is an enzyme in the family of transferases that catalyzes the chemical reaction ATP + pyruvate + phosphate ⇌ {\displaystyle \rightleftharpoons } AMP + phosphoenolpyruvate + diphosphate