NADPH-dependent medium chain alcohol dehydrogenase; has broad substrate specificity; member of the cinnamyl family of alcohol dehydrogenases; may be involved in fusel alcohol synthesis or in aldehyde tolerance; protein abundance increases in response to DNA replication stress.

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.

NADPH-dependent medium chain alcohol dehydrogenase; has broad substrate specificity; member of the cinnamyl family of alcohol dehydrogenases; may be involved in fusel alcohol synthesis or in aldehyde tolerance; protein abundance increases in response to DNA replication stress.

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.

NADPH-dependent medium chain alcohol dehydrogenase; has broad substrate specificity; member of the cinnamyl family of alcohol dehydrogenases; may be involved in fusel alcohol synthesis or in aldehyde tolerance; protein abundance increases in response to DNA replication stress.

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.

NADPH-dependent medium chain alcohol dehydrogenase; has broad substrate specificity; member of the cinnamyl family of alcohol dehydrogenases; may be involved in fusel alcohol synthesis or in aldehyde tolerance; protein abundance increases in response to DNA replication stress.

Sorbitol dehydrogenase; protein sequence is 99% identical to the Sor2p sorbitol dehydrogenase; expression is induced in the presence of sorbitol or xylose; Belongs to the zinc-containing alcohol dehydrogenase family.

NADPH-dependent medium chain alcohol dehydrogenase; has broad substrate specificity; member of the cinnamyl family of alcohol dehydrogenases; may be involved in fusel alcohol synthesis or in aldehyde tolerance; protein abundance increases in response to DNA replication stress.

Sorbitol dehydrogenase; protein sequence is 99% identical to the Sor1p sorbitol dehydrogenase.

NADPH-dependent medium chain alcohol dehydrogenase; has broad substrate specificity; member of the cinnamyl family of alcohol dehydrogenases; may be involved in fusel alcohol synthesis or in aldehyde tolerance; protein abundance increases in response to DNA replication stress.

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.

NADPH-dependent medium chain alcohol dehydrogenase; has broad substrate specificity; member of the cinnamyl family of alcohol dehydrogenases; may be involved in fusel alcohol synthesis or in aldehyde tolerance; protein abundance increases in response to DNA replication stress.

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.

Metallothionein; binds copper and mediates resistance to high concentrations of copper and cadmium; locus is variably amplified in different strains, with two copies, CUP1-1 and CUP1-2, in the genomic sequence reference strain S288C; CUP1-1 has a paralog, CUP1-2, that arose from a segmental duplication.

Metallothionein; binds copper and mediates resistance to high concentrations of copper and cadmium; locus is variably amplified in different strains, with two copies, CUP1-1 and CUP1-2, in the genomic sequence reference strain S288C; CUP1-2 has a paralog, CUP1-1, that arose from a segmental duplication.

Metallothionein; binds copper and mediates resistance to high concentrations of copper and cadmium; locus is variably amplified in different strains, with two copies, CUP1-1 and CUP1-2, in the genomic sequence reference strain S288C; CUP1-2 has a paralog, CUP1-1, that arose from a segmental duplication.

Metallothionein; binds copper and mediates resistance to high concentrations of copper and cadmium; locus is variably amplified in different strains, with two copies, CUP1-1 and CUP1-2, in the genomic sequence reference strain S288C; CUP1-1 has a paralog, CUP1-2, that arose from a segmental duplication.

Cyanamide hydratase that detoxifies cyanamide; member of the HD domain metalloprotein superfamily; expression is induced over 100-fold by cyanamide and by SN2-type DNA alkylating agents such as MMS and DMA; induction decreased in rad6 and rad18 mutants; gene and protein are identical to DDI3 and Ddi3p.

Cyanamide hydratase that detoxifies cyanamide; member of the HD domain metalloprotein superfamily; expression is induced over 100-fold by cyanamide and by SN2-type DNA alkylating agents such as MMS and DMA; induction decreased in rad6 and rad18 mutants; gene and protein are identical to DDI2 and Ddi2p.

Cyanamide hydratase that detoxifies cyanamide; member of the HD domain metalloprotein superfamily; expression is induced over 100-fold by cyanamide and by SN2-type DNA alkylating agents such as MMS and DMA; induction decreased in rad6 and rad18 mutants; gene and protein are identical to DDI2 and Ddi2p.

Cyanamide hydratase that detoxifies cyanamide; member of the HD domain metalloprotein superfamily; expression is induced over 100-fold by cyanamide and by SN2-type DNA alkylating agents such as MMS and DMA; induction decreased in rad6 and rad18 mutants; gene and protein are identical to DDI3 and Ddi3p.

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.

NADPH-dependent medium chain alcohol dehydrogenase; has broad substrate specificity; member of the cinnamyl family of alcohol dehydrogenases; may be involved in fusel alcohol synthesis or in aldehyde tolerance; protein abundance increases in response to DNA replication stress.

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.

Ubiquitin carboxyl-terminal hydrolase RPN11; Metalloprotease subunit of 19S regulatory particle; part of 26S proteasome lid; couples the deubiquitination and degradation of proteasome substrates; involved, independent of catalytic activity, in fission of mitochondria and peroxisomes; protein abundance increases in response to DNA replication stress.

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.

Sorbitol dehydrogenase; protein sequence is 99% identical to the Sor2p sorbitol dehydrogenase; expression is induced in the presence of sorbitol or xylose; Belongs to the zinc-containing alcohol dehydrogenase 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.

Sorbitol dehydrogenase; protein sequence is 99% identical to the Sor1p sorbitol dehydrogenase.

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.