Cys-Gly metallodipeptidase DUG1; Cys-Gly metallo-di-peptidase; forms a complex with Dug2p and Dug3p to degrade glutathione (GSH) and other peptides containing a gamma-glu-X bond in an alternative pathway to GSH degradation by gamma-glutamyl transpeptidase (Ecm38p); human homolog CNDP2 can complement yeast dug1 mutant.

Glutamate--cysteine ligase; Gamma glutamylcysteine synthetase; catalyzes the first step in glutathione (GSH) biosynthesis; expression induced by oxidants, cadmium, and mercury; protein abundance increases in response to DNA replication stress; Belongs to the glutamate--cysteine ligase type 3 family.

Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress.

Nitrogen catabolite repression transcriptional regulator; inhibits GLN3 transcription in good nitrogen source; role in sequestering Gln3p and Gat1p to the cytoplasm; has glutathione peroxidase activity and can mutate to acquire GST activity; self-assembly under limited nitrogen conditions creates [URE3] prion and releases catabolite repression.

Glutathione-specific gamma-glutamylcyclotransferase; Gamma-glutamyl cyclotransferase; cleaves the gamma-glutamyl bond of glutathione to yield 5-oxoproline and a Cys-Gly dipeptide; similar to mammalian pro-apoptotic protein ChaC1; expression of mouse ChaC1 in yeast increases apoptosis; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm and nucleus; periodically expressed during the metabolic cycle.

ER associated glutathione S-transferase; capable of homodimerization; glutathione transferase for Yvc1p vacuolar cation channel; expression induced during the diauxic shift and throughout stationary phase; functional overlap with Gtt2p, Grx1p, and Grx2p.

Probable alanine aminotransferase; Catalytically inactive alanine transaminase; expression is repressed in the presence of alanine and repression is mediated by Nrg1p; ALT2 has a paralog, ALT1, that arose from the whole genome duplication; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.

Probable alanine aminotransferase, mitochondrial; Alanine transaminase (glutamic pyruvic transaminase); involved in alanine biosynthesis and catabolism; TOR1-independent role in determining chronological lifespan; expression is induced in the presence of alanine; repression is mediated by Nrg1p; ALT1 has a paralog, ALT2, that arose from the whole genome duplication; Alt2p is catalytically inactive; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.

Mitochondrial peroxiredoxin with thioredoxin peroxidase activity; has a role in reduction of hydroperoxides; reactivation requires Trr2p and glutathione; induced during respiratory growth and oxidative stress; phosphorylated; protein abundance increases in response to DNA replication stress.