Transaminated amino acid decarboxylase; Phenylpyruvate decarboxylase; catalyzes decarboxylation of phenylpyruvate to phenylacetaldehyde, which is the first specific step in the Ehrlich pathway; involved in protein N-terminal Met and Ala catabolism.

Acetolactate synthase catalytic subunit, mitochondrial; Acetolactate synthase; catalyses the first common step in isoleucine and valine biosynthesis and is the target of several classes of inhibitors, localizes to the mitochondria; expression of the gene is under general amino acid control; Belongs to the TPP enzyme family.

NAD-dependent protein deacetylase HST1; NAD(+)-dependent histone deacetylase; essential subunit of the Sum1p/Rfm1p/Hst1p complex required for ORC-dependent silencing and meiotic repression; non-essential subunit of the Set3C deacetylase complex; involved in telomere maintenance; HST1 has a paralog, SIR2, that arose from the whole genome duplication.

Cytoplasmic NAD(+)-dependent protein deacetylase; deacetylation targets are primarily cytoplasmic proteins; member of the silencing information regulator 2 (Sir2) family of NAD(+)-dependent protein deacetylases; modulates nucleolar (rDNA) and telomeric silencing; possesses NAD(+)-dependent histone deacetylase activity in vitro; contains a nuclear export signal (NES); function regulated by its nuclear export; Belongs to the sirtuin family. Class I subfamily.

NAD-dependent protein deacetylase HST1; NAD(+)-dependent histone deacetylase; essential subunit of the Sum1p/Rfm1p/Hst1p complex required for ORC-dependent silencing and meiotic repression; non-essential subunit of the Set3C deacetylase complex; involved in telomere maintenance; HST1 has a paralog, SIR2, that arose from the whole genome duplication.

Conserved NAD+ dependent histone deacetylase of the Sirtuin family; deacetylation targets are primarily nuclear proteins; required for telomere hypercluster formation in quiescent yeast cells; involved in regulation of lifespan; plays roles in silencing at HML, HMR, telomeres, and rDNA; negatively regulates initiation of DNA replication; functions as regulator of autophagy like mammalian homolog SIRT1, and also of mitophagy.

Cytoplasmic NAD(+)-dependent protein deacetylase; deacetylation targets are primarily cytoplasmic proteins; member of the silencing information regulator 2 (Sir2) family of NAD(+)-dependent protein deacetylases; modulates nucleolar (rDNA) and telomeric silencing; possesses NAD(+)-dependent histone deacetylase activity in vitro; contains a nuclear export signal (NES); function regulated by its nuclear export; Belongs to the sirtuin family. Class I subfamily.

NAD-dependent protein deacetylase HST1; NAD(+)-dependent histone deacetylase; essential subunit of the Sum1p/Rfm1p/Hst1p complex required for ORC-dependent silencing and meiotic repression; non-essential subunit of the Set3C deacetylase complex; involved in telomere maintenance; HST1 has a paralog, SIR2, that arose from the whole genome duplication.

Cytoplasmic NAD(+)-dependent protein deacetylase; deacetylation targets are primarily cytoplasmic proteins; member of the silencing information regulator 2 (Sir2) family of NAD(+)-dependent protein deacetylases; modulates nucleolar (rDNA) and telomeric silencing; possesses NAD(+)-dependent histone deacetylase activity in vitro; contains a nuclear export signal (NES); function regulated by its nuclear export; Belongs to the sirtuin family. Class I subfamily.

NAD-dependent histone deacetylase HST3; Member of the Sir2 family of NAD(+)-dependent protein deacetylases; involved along with Hst4p in telomeric silencing, cell cycle progression, radiation resistance, genomic stability and short-chain fatty acid metabolism.

Cytoplasmic NAD(+)-dependent protein deacetylase; deacetylation targets are primarily cytoplasmic proteins; member of the silencing information regulator 2 (Sir2) family of NAD(+)-dependent protein deacetylases; modulates nucleolar (rDNA) and telomeric silencing; possesses NAD(+)-dependent histone deacetylase activity in vitro; contains a nuclear export signal (NES); function regulated by its nuclear export; Belongs to the sirtuin family. Class I subfamily.

NAD-dependent histone deacetylase HST4; NAD(+)-dependent protein deacetylase; deacetylation targets are primarily mitochondrial proteins; involved along with Hst3p in silencing at telomeres, cell cycle progression, radiation resistance, genomic stability and short-chain fatty acid metabolism; accumulates in mitochondria in response to biotin starvation and may link biotin metabolism with energy homeostasis; member of the Sir2 family and may be the functional equivalent of human SIRT3.

Cytoplasmic NAD(+)-dependent protein deacetylase; deacetylation targets are primarily cytoplasmic proteins; member of the silencing information regulator 2 (Sir2) family of NAD(+)-dependent protein deacetylases; modulates nucleolar (rDNA) and telomeric silencing; possesses NAD(+)-dependent histone deacetylase activity in vitro; contains a nuclear export signal (NES); function regulated by its nuclear export; Belongs to the sirtuin family. Class I subfamily.

Conserved NAD+ dependent histone deacetylase of the Sirtuin family; deacetylation targets are primarily nuclear proteins; required for telomere hypercluster formation in quiescent yeast cells; involved in regulation of lifespan; plays roles in silencing at HML, HMR, telomeres, and rDNA; negatively regulates initiation of DNA replication; functions as regulator of autophagy like mammalian homolog SIRT1, and also of mitophagy.

NAD-dependent histone deacetylase HST3; Member of the Sir2 family of NAD(+)-dependent protein deacetylases; involved along with Hst4p in telomeric silencing, cell cycle progression, radiation resistance, genomic stability and short-chain fatty acid metabolism.

Cytoplasmic NAD(+)-dependent protein deacetylase; deacetylation targets are primarily cytoplasmic proteins; member of the silencing information regulator 2 (Sir2) family of NAD(+)-dependent protein deacetylases; modulates nucleolar (rDNA) and telomeric silencing; possesses NAD(+)-dependent histone deacetylase activity in vitro; contains a nuclear export signal (NES); function regulated by its nuclear export; Belongs to the sirtuin family. Class I subfamily.

NAD-dependent histone deacetylase HST3; Member of the Sir2 family of NAD(+)-dependent protein deacetylases; involved along with Hst4p in telomeric silencing, cell cycle progression, radiation resistance, genomic stability and short-chain fatty acid metabolism.

NAD-dependent histone deacetylase HST4; NAD(+)-dependent protein deacetylase; deacetylation targets are primarily mitochondrial proteins; involved along with Hst3p in silencing at telomeres, cell cycle progression, radiation resistance, genomic stability and short-chain fatty acid metabolism; accumulates in mitochondria in response to biotin starvation and may link biotin metabolism with energy homeostasis; member of the Sir2 family and may be the functional equivalent of human SIRT3.

NAD-dependent histone deacetylase HST3; Member of the Sir2 family of NAD(+)-dependent protein deacetylases; involved along with Hst4p in telomeric silencing, cell cycle progression, radiation resistance, genomic stability and short-chain fatty acid metabolism.

Conserved NAD+ dependent histone deacetylase of the Sirtuin family; deacetylation targets are primarily nuclear proteins; required for telomere hypercluster formation in quiescent yeast cells; involved in regulation of lifespan; plays roles in silencing at HML, HMR, telomeres, and rDNA; negatively regulates initiation of DNA replication; functions as regulator of autophagy like mammalian homolog SIRT1, and also of mitophagy.

NAD-dependent histone deacetylase HST4; NAD(+)-dependent protein deacetylase; deacetylation targets are primarily mitochondrial proteins; involved along with Hst3p in silencing at telomeres, cell cycle progression, radiation resistance, genomic stability and short-chain fatty acid metabolism; accumulates in mitochondria in response to biotin starvation and may link biotin metabolism with energy homeostasis; member of the Sir2 family and may be the functional equivalent of human SIRT3.

Cytoplasmic NAD(+)-dependent protein deacetylase; deacetylation targets are primarily cytoplasmic proteins; member of the silencing information regulator 2 (Sir2) family of NAD(+)-dependent protein deacetylases; modulates nucleolar (rDNA) and telomeric silencing; possesses NAD(+)-dependent histone deacetylase activity in vitro; contains a nuclear export signal (NES); function regulated by its nuclear export; Belongs to the sirtuin family. Class I subfamily.

NAD-dependent histone deacetylase HST4; NAD(+)-dependent protein deacetylase; deacetylation targets are primarily mitochondrial proteins; involved along with Hst3p in silencing at telomeres, cell cycle progression, radiation resistance, genomic stability and short-chain fatty acid metabolism; accumulates in mitochondria in response to biotin starvation and may link biotin metabolism with energy homeostasis; member of the Sir2 family and may be the functional equivalent of human SIRT3.

NAD-dependent histone deacetylase HST3; Member of the Sir2 family of NAD(+)-dependent protein deacetylases; involved along with Hst4p in telomeric silencing, cell cycle progression, radiation resistance, genomic stability and short-chain fatty acid metabolism.

NAD-dependent histone deacetylase HST4; NAD(+)-dependent protein deacetylase; deacetylation targets are primarily mitochondrial proteins; involved along with Hst3p in silencing at telomeres, cell cycle progression, radiation resistance, genomic stability and short-chain fatty acid metabolism; accumulates in mitochondria in response to biotin starvation and may link biotin metabolism with energy homeostasis; member of the Sir2 family and may be the functional equivalent of human SIRT3.

Conserved NAD+ dependent histone deacetylase of the Sirtuin family; deacetylation targets are primarily nuclear proteins; required for telomere hypercluster formation in quiescent yeast cells; involved in regulation of lifespan; plays roles in silencing at HML, HMR, telomeres, and rDNA; negatively regulates initiation of DNA replication; functions as regulator of autophagy like mammalian homolog SIRT1, and also of mitophagy.

Acetolactate synthase catalytic subunit, mitochondrial; Acetolactate synthase; catalyses the first common step in isoleucine and valine biosynthesis and is the target of several classes of inhibitors, localizes to the mitochondria; expression of the gene is under general amino acid control; Belongs to the TPP enzyme family.

Transaminated amino acid decarboxylase; Phenylpyruvate decarboxylase; catalyzes decarboxylation of phenylpyruvate to phenylacetaldehyde, which is the first specific step in the Ehrlich pathway; involved in protein N-terminal Met and Ala 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.

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.

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.