| glutathione—homocystine transhydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.8.4.1 | ||||||||
| CAS no. | 9029-40-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a glutathione—homocystine transhydrogenase (EC 1.8.4.1) is an enzyme that catalyzes the chemical reaction
- 2 glutathione + homocystine glutathione disulfide + 2 homocysteine
Thus, the two substrates of this enzyme are glutathione and homocystine, whereas its two products are glutathione disulfide and homocysteine.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is glutathione:homocystine oxidoreductase. This enzyme participates in methionine metabolism and glutathione metabolism.
References
- Racker, E. (December 1955). "Glutathione-homocystine transhydrogenase". Journal of Biological Chemistry. 217 (2): 867–874. doi:10.1016/s0021-9258(18)65951-4. ISSN 0021-9258. PMID 13271447.
This page was last edited on 1 January 2024, at 04:09