Structural highlights
Function
NCPPR_PYRHO Catalyzes the NAD(P)H-dependent reduction of polysulfide, CoA-polysulfides, and CoA persulfide, as well as the reduction of a range of other small persulfides, including TNB and glutathione persulfides. The likely in vivo substrates are di-, poly-, and persulfide derivatives of coenzyme A, although polysulfide itself is also efficiently reduced (PubMed:23530771). Shows coenzyme A disulfide reductase (CoADR) activity with both NADH and NADPH, with a preference for NADPH (PubMed:15720393). May also play a role in the reduction of elemental sulfur (PubMed:23530771).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Harris DR, Ward DE, Feasel JM, Lancaster KM, Murphy RD, Mallet TC, Crane EJ 3rd. Discovery and characterization of a Coenzyme A disulfide reductase from Pyrococcus horikoshii. Implications for this disulfide metabolism of anaerobic hyperthermophiles. FEBS J. 2005 Mar;272(5):1189-200. PMID:15720393 doi:EJB4555
- ↑ Herwald S, Liu AY, Zhu BE, Sea KW, Lopez KM, Sazinsky MH, Crane Iii EJ. Characterization of the structure and substrate specificity of the pyrococcal CoADR/Psr: Implications for S0-based respiration and a sulfur-dependent antioxidant system in Pyrococcus. Biochemistry. 2013 Mar 26. PMID:23530771 doi:10.1021/bi3014399
