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Pyruvate decarboxylase is an enzyme (EC 4.1.1.1) that catalyses the decarboxylation of pyruvic acid to acetaldehyde. It is also called 2-oxo-acid carboxylase, alpha-ketoacid carboxylase, and pyruvic decarboxylase. [ 1 ]
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 ...
Aromatic-L-amino-acid decarboxylase; Glutamate decarboxylase; Histidine decarboxylase; Ornithine decarboxylase; Phosphoenolpyruvate carboxylase; Pyruvate decarboxylase; RuBisCO – the only carboxylase that leads to a net fixation of carbon dioxide; Uridine monophosphate synthetase; Uroporphyrinogen III decarboxylase; enoyl-CoA carboxylases ...
Pyruvate, for example, undergoes both types of decarboxylation, both involving TPP. In fermentative organisms, pyruvate is non-oxidatively decarboxylated by the TPP-dependent enzyme pyruvate decarboxylase. As part of the PDH complex, TPP assists in oxidative decarboxylation of pyruvate. TPP is a true catalytic cofactor.
In several reactions, including that of pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase, and transketolase, TPP catalyses the reversible decarboxylation reaction (aka cleavage of a substrate compound at a carbon-carbon bond connecting a carbonyl group to an adjacent reactive group—usually a carboxylic acid or an alcohol).
The enzyme indolepyruvate decarboxylase (EC 4.1.1.74) catalyzes the chemical reaction 3-(indol-3-yl)pyruvate ⇌ {\displaystyle \rightleftharpoons } 2-(indol-3-yl)acetaldehyde + CO 2 This enzyme belongs to the family of lyases , specifically the carboxy-lyases, which cleave carbon-carbon bonds.
Pyruvate decarboxylation requires a few cofactors in addition to the enzymes that make up the complex. The first is thiamine pyrophosphate (TPP), which is used by pyruvate dehydrogenase to oxidize pyruvate and to form a hydroxyethyl-TPP intermediate. This intermediate is taken up by dihydrolipoyl transacetylase and reacted with a second ...