Trypanothione-disulfide reductase

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In enzymology, a trypanothione-disulfide reductase (EC 1.8.1.12) is an enzyme that catalyzes the chemical reaction

trypanothione + NADP⁺ $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 1.8.1.12
BRENDA references for 1.8.1.12 (Recommended.)
PubMed references for 1.8.1.12
PubMed Central references for 1.8.1.12
Google Scholar references for 1.8.1.12
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: 3519–26. doi:10.1021/bi00360a007. PMID 3718941.
Marsh IR, Bradley M (1997). "Substrate specificity of trypanothione reductase". Eur. J. Biochem. 243: 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: 460–8. doi:10.1111/j.1432-1033.1995.tb20583.x. PMID 7607216.