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.

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.

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.

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.

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.

Minor isoform of pyruvate decarboxylase; decarboxylates pyruvate to acetaldehyde, involved in amino acid catabolism; transcription is glucose- and ethanol-dependent, and is strongly induced during sulfur limitation; Belongs to the TPP enzyme family.

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.

Thiamine metabolism regulatory protein THI3; Regulatory protein that binds Pdc2p and Thi2p transcription factors; activates thiamine biosynthesis transcription factors Pdc2p and Thi2p by binding to them, but releases and de-activates them upon binding to thiamine pyrophosphate (TPP), the end product of the pathway; has similarity to decarboxylases but enzymatic activity is not detected.

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.

Transketolase; catalyzes conversion of xylulose-5-phosphate and ribose-5-phosphate to sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate in the pentose phosphate pathway; needed for synthesis of aromatic amino acids; TKL1 has a paralog, TKL2, that arose from the whole genome duplication.

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.

Transketolase; catalyzes conversion of xylulose-5-phosphate and ribose-5-phosphate to sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate in the pentose phosphate pathway; needed for synthesis of aromatic amino acids; TKL2 has a paralog, TKL1, that arose from the whole genome duplication.

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.

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.

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.

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.

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.

Minor isoform of pyruvate decarboxylase; decarboxylates pyruvate to acetaldehyde, involved in amino acid catabolism; transcription is glucose- and ethanol-dependent, and is strongly induced during sulfur limitation; Belongs to the TPP enzyme family.

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.

Thiamine metabolism regulatory protein THI3; Regulatory protein that binds Pdc2p and Thi2p transcription factors; activates thiamine biosynthesis transcription factors Pdc2p and Thi2p by binding to them, but releases and de-activates them upon binding to thiamine pyrophosphate (TPP), the end product of the pathway; has similarity to decarboxylases but enzymatic activity is not detected.

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.

Transketolase; catalyzes conversion of xylulose-5-phosphate and ribose-5-phosphate to sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate in the pentose phosphate pathway; needed for synthesis of aromatic amino acids; TKL1 has a paralog, TKL2, that arose from the whole genome duplication.

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.

Transketolase; catalyzes conversion of xylulose-5-phosphate and ribose-5-phosphate to sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate in the pentose phosphate pathway; needed for synthesis of aromatic amino acids; TKL2 has a paralog, TKL1, 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.

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.

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.

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.

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.

Minor isoform of pyruvate decarboxylase; decarboxylates pyruvate to acetaldehyde, involved in amino acid catabolism; transcription is glucose- and ethanol-dependent, and is strongly induced during sulfur limitation; Belongs to the TPP enzyme family.

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.

Thiamine metabolism regulatory protein THI3; Regulatory protein that binds Pdc2p and Thi2p transcription factors; activates thiamine biosynthesis transcription factors Pdc2p and Thi2p by binding to them, but releases and de-activates them upon binding to thiamine pyrophosphate (TPP), the end product of the pathway; has similarity to decarboxylases but enzymatic activity is not detected.

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.

Transketolase; catalyzes conversion of xylulose-5-phosphate and ribose-5-phosphate to sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate in the pentose phosphate pathway; needed for synthesis of aromatic amino acids; TKL1 has a paralog, TKL2, 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.

Transketolase; catalyzes conversion of xylulose-5-phosphate and ribose-5-phosphate to sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate in the pentose phosphate pathway; needed for synthesis of aromatic amino acids; TKL2 has a paralog, TKL1, that arose from the whole genome duplication.

Minor isoform of pyruvate decarboxylase; decarboxylates pyruvate to acetaldehyde, involved in amino acid catabolism; transcription is glucose- and ethanol-dependent, and is strongly induced during sulfur limitation; Belongs to the TPP enzyme family.

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.

Minor isoform of pyruvate decarboxylase; decarboxylates pyruvate to acetaldehyde, involved in amino acid catabolism; transcription is glucose- and ethanol-dependent, and is strongly induced during sulfur limitation; Belongs to the TPP enzyme family.

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.