Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

Cytoplasmic aldehyde dehydrogenase; involved in beta-alanine synthesis; uses NAD+ as the preferred coenzyme; very similar to Ald2p; expression is induced by stress and repressed by glucose.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

Mitochondrial aldehyde dehydrogenase; required for growth on ethanol and conversion of acetaldehyde to acetate; phosphorylated; activity is K+ dependent; utilizes NADP+ or NAD+ equally as coenzymes; expression is glucose repressed; can substitute for cytosolic NADP-dependent aldehyde dehydrogenase when directed to the cytosol; human homolog ALDH2 can complement yeast ald4 mutant.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

Cytosolic aldehyde dehydrogenase; activated by Mg2+ and utilizes NADP+ as the preferred coenzyme; required for conversion of acetaldehyde to acetate; constitutively expressed; locates to the mitochondrial outer surface upon oxidative stress.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

Isocitrate lyase; catalyzes the formation of succinate and glyoxylate from isocitrate, a key reaction of the glyoxylate cycle; expression of ICL1 is induced by growth on ethanol and repressed by growth on glucose.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

2-methylisocitrate lyase of the mitochondrial matrix; functions in the methylcitrate cycle to catalyze the conversion of 2-methylisocitrate to succinate and pyruvate; ICL2 transcription is repressed by glucose and induced by ethanol.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

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.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

E1 alpha subunit of the pyruvate dehydrogenase (PDH) complex; catalyzes the direct oxidative decarboxylation of pyruvate to acetyl-CoA; phosphorylated; regulated by glucose; PDH complex is concentrated in spots within the mitochondrial matrix, often near the ERMES complex and near peroxisomes.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

E1 beta subunit of the pyruvate dehydrogenase (PDH) complex; PDH is an evolutionarily conserved multi-protein complex found in mitochondria.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

Pyruvate carboxylase isoform; cytoplasmic enzyme that converts pyruvate to oxaloacetate; differentially regulated than isoform Pyc2p; mutations in the human homolog are associated with lactic acidosis; PYC1 has a paralog, PYC2, that arose from the whole genome duplication.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

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.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

Glucose-6-phosphate dehydrogenase (G6PD); catalyzes the first step of the pentose phosphate pathway; involved in adapting to oxidative stress; protein abundance increases in response to DNA replication stress; homolog of human G6PD which is deficient in patients with hemolytic anemia; human G6PD can complement yeast zwf1 null mutant.

Cytoplasmic aldehyde dehydrogenase; involved in beta-alanine synthesis; uses NAD+ as the preferred coenzyme; very similar to Ald2p; expression is induced by stress and repressed by glucose.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

Cytoplasmic aldehyde dehydrogenase; involved in beta-alanine synthesis; uses NAD+ as the preferred coenzyme; very similar to Ald2p; expression is induced by stress and repressed by glucose.

Mitochondrial aldehyde dehydrogenase; required for growth on ethanol and conversion of acetaldehyde to acetate; phosphorylated; activity is K+ dependent; utilizes NADP+ or NAD+ equally as coenzymes; expression is glucose repressed; can substitute for cytosolic NADP-dependent aldehyde dehydrogenase when directed to the cytosol; human homolog ALDH2 can complement yeast ald4 mutant.

Cytoplasmic aldehyde dehydrogenase; involved in beta-alanine synthesis; uses NAD+ as the preferred coenzyme; very similar to Ald2p; expression is induced by stress and repressed by glucose.

Isocitrate lyase; catalyzes the formation of succinate and glyoxylate from isocitrate, a key reaction of the glyoxylate cycle; expression of ICL1 is induced by growth on ethanol and repressed by growth on glucose.

Cytoplasmic aldehyde dehydrogenase; involved in beta-alanine synthesis; uses NAD+ as the preferred coenzyme; very similar to Ald2p; expression is induced by stress and repressed by glucose.

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.

Cytoplasmic aldehyde dehydrogenase; involved in beta-alanine synthesis; uses NAD+ as the preferred coenzyme; very similar to Ald2p; expression is induced by stress and repressed by glucose.

Malate synthase, enzyme of the glyoxylate cycle; involved in utilization of non-fermentable carbon sources; expression is subject to carbon catabolite repression; localizes in peroxisomes during growth on oleic acid, otherwise cytosolic; can accept butyryl-CoA as acyl-CoA donor in addition to traditional substrate acetyl-CoA.

Cytoplasmic aldehyde dehydrogenase; involved in beta-alanine synthesis; uses NAD+ as the preferred coenzyme; very similar to Ald2p; expression is induced by stress and repressed by glucose.

E1 alpha subunit of the pyruvate dehydrogenase (PDH) complex; catalyzes the direct oxidative decarboxylation of pyruvate to acetyl-CoA; phosphorylated; regulated by glucose; PDH complex is concentrated in spots within the mitochondrial matrix, often near the ERMES complex and near peroxisomes.

Cytoplasmic aldehyde dehydrogenase; involved in beta-alanine synthesis; uses NAD+ as the preferred coenzyme; very similar to Ald2p; expression is induced by stress and repressed by glucose.

E1 beta subunit of the pyruvate dehydrogenase (PDH) complex; PDH is an evolutionarily conserved multi-protein complex found in mitochondria.

Cytoplasmic aldehyde dehydrogenase; involved in beta-alanine synthesis; uses NAD+ as the preferred coenzyme; very similar to Ald2p; expression is induced by stress and repressed by glucose.

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.

Cytoplasmic aldehyde dehydrogenase; involved in beta-alanine synthesis; uses NAD+ as the preferred coenzyme; very similar to Ald2p; expression is induced by stress and repressed by glucose.

Pyruvate carboxylase isoform; cytoplasmic enzyme that converts pyruvate to oxaloacetate; differentially regulated than isoform Pyc2p; mutations in the human homolog are associated with lactic acidosis; PYC1 has a paralog, PYC2, that arose from the whole genome duplication.