| Thiol:disulfide interchange protein DsbC | Escherichia coli (strain K12) | Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. Ds... more | 1 | Details |
| Thiopurine S-methyltransferase | Humans | Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine (also called mercaptopurine, 6-MP or its bra... more | 8 | Details |
| Thioredoxin | Alicyclobacillus acidocaldarius | Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide ... more | 3 | Details |
| Thioredoxin | Humans | Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide ... more | 3 | Details |
| Thioredoxin reductase | Mouse | Not Available | 1 | Details |
| Thioredoxin reductase | Staphylococcus aureus (strain Mu50 / ATCC 700699) | Not Available | 3 | Details |
| Thioredoxin reductase | Escherichia coli (strain K12) | Not Available | 1 | Details |
| Thioredoxin reductase 1, cytoplasmic | Humans | Reduces disulfide protein thioredoxin (Trx) to its dithiol-containing form. Homodimeric flavoprotein involved in the ... more | 23 | Details |
| Thioredoxin reductase 2, mitochondrial | Humans | Involved in the control of reactive oxygen species levels and the regulation of mitochondrial redox homeostasis. Main... more | 3 | Details |
| Thioredoxin-interacting protein | Humans | May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Intera... more | 1 | Details |
| Thioredoxin-like protein 1 | Plasmodium falciparum (isolate 3D7) | Not Available | 1 | Details |
| Thioredoxin-related protein, putative | Plasmodium falciparum (isolate 3D7) | Not Available | 1 | Details |
| Thiostrepton | Streptomyces azureus | Has bacteriocidal activity. Inhibits bacterial protein biosynthesis by acting on the elongation factor Tu (EF-Tu). | 2 | Details |
| Thiosulfate reductase | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) | Not Available | 1 | Details |
| Thiosulfate sulfurtransferase | Humans | Catalyzes the transfer of sulfur ion from thiosulfate to cyanide, although other thiol compounds, besides cyanide, ca... more | 3 | Details |
| Thiosulfate sulfurtransferase | Azotobacter vinelandii | Not Available | 1 | Details |
| Thiosulfate sulfurtransferase GlpE | Shigella flexneri | Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. | 1 | Details |
| Thiosulfate:glutathione sulfurtransferase | Humans | Thiosulfate:glutathione sulfurtransferase (TST) required to produce S-sulfanylglutathione (GSS(-)), a central interme... more | 2 | Details |
| Threonine--tRNA ligase | Staphylococcus aureus (strain MW2) | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to f... more | 1 | Details |
| Threonine--tRNA ligase | Shigella flexneri | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to f... more | 3 | Details |
| Threonine--tRNA ligase | Plasmodium falciparum (isolate 3D7) | Not Available | 1 | Details |
| Threonine--tRNA ligase 1, cytoplasmic | Humans | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to for... more | 2 | Details |
| Threonine--tRNA ligase, mitochondrial | Humans | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to for... more | 1 | Details |
| Threonine-phosphate decarboxylase | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage... more | 2 | Details |
| Thrombomodulin | Humans | Endothelial cell receptor that plays a critical role in regulating several physiological processes including hemostas... more | 3 | Details |