Trypanothione-disulfide reductase
In enzymology, a trypanothione-disulfide reductase (EC 1.8.1.12) is an enzyme that catalyzes the chemical reaction
- trypanothione + NADP+ trypanothione disulfide + NADPH + H+
Thus, the two substrates of this enzyme are trypanothione and NADP+, whereas its 3 products are trypanothione disulfide, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is trypanothione:NADP+ oxidoreductase. Other names in common use include trypanothione reductase, and NADPH2:trypanothione oxidoreductase. It employs one cofactor, FAD.
References
- Shames SL, Fairlamb AH, Cerami A, Walsh CT (1986). "Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases". Biochemistry. 25 (12): 3519–26. doi:10.1021/bi00360a007. PMID 3718941.
- Marsh IR, Bradley M (1997). "Substrate specificity of trypanothione reductase". Eur. J. Biochem. 243 (3): 690–4. doi:10.1111/j.1432-1033.1997.00690.x. PMID 9057833.
- Cunningham ML, Fairlamb AH (1995). "Trypanothione reductase from Leishmania donovani. Purification, characterisation and inhibition by trivalent antimonials". Eur. J. Biochem. 230 (2): 460–8. doi:10.1111/j.1432-1033.1995.tb20583.x. PMID 7607216.
- Stump B, Kaiser M, Brun R, Krauth-Siegel RL, Diederich F (2007). "Betraying the Parasites Redox System: Diaryl Sulfide-Based Inhibitors of Trypanothione Reductase: Subversive Substrates and Antitrypanosomal Properties". ChemMedChem 2 (12): 1708–12. doi:10.1002/cmdc.200700172. PMID 17918760.
|
---|
| Activity | |
---|
| Regulation | |
---|
| Classification | |
---|
| Types | |
---|
|