Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; the lipoamide dehydrogenase component (E3) of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase multi-enzyme complexes; PDH complex is concentrated in spots within the mitochondrial matrix, often near the ERMES complex and near peroxisomes; LPD1 has a paralog, IRC15, that arose from the whole genome duplication; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

E3-binding protein of the mitochondrial pyruvate dehydrogenase complex; plays a structural role in the complex by binding and positioning dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide acetyltransferase (E2) core.

Dihydrolipoamide acetyltransferase component (E2) of the PDC; the pyruvate dehydrogenase complex (PDC) catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA.

Pyruvate kinase; functions as a homotetramer in glycolysis to convert phosphoenolpyruvate to pyruvate, the input for aerobic (TCA cycle) or anaerobic (glucose fermentation) respiration; regulated via allosteric activation by fructose bisphosphate; CDC19 has a paralog, PYK2, that arose from the whole genome duplication.

Glycolytic enzyme phosphoglucose isomerase; catalyzes the interconversion of glucose-6-phosphate and fructose-6-phosphate; required for cell cycle progression and completion of the gluconeogenic events of sporulation.

Major of three pyruvate decarboxylase isozymes; key enzyme in alcoholic fermentation; decarboxylates pyruvate to acetaldehyde; involved in amino acid catabolism; subject to glucose-, ethanol-, and autoregulation; activated by phosphorylation in response to glucose levels; N-terminally propionylated in vivo; Belongs to the TPP enzyme family.

Mitochondrial malic enzyme; catalyzes the oxidative decarboxylation of malate to pyruvate, which is a key intermediate in sugar metabolism and a precursor for synthesis of several amino acids.

Pyruvate carboxylase isoform; cytoplasmic enzyme that converts pyruvate to oxaloacetate; differentially regulated than isoform Pyc1p; mutations in the human homolog are associated with lactic acidosis; PYC2 has a paralog, PYC1, that arose from the whole genome duplication.

Minor isoform of pyruvate decarboxylase; key enzyme in alcoholic fermentation, decarboxylates pyruvate to acetaldehyde, regulation is glucose- and ethanol-dependent, repressed by thiamine, involved in amino acid catabolism.