“Trypanothione-disulfide reductase”的意思、由来-开放百科全书

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

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.

The X-ray crystal structures of trypanothione reductase enzymes from several trypanosomatids species have been solved, including those from Crithidia fasciculata, Leishmania infantum, Trypanosoma brucei and Trypanosoma cruzi. The structures reveal that trypanothione reductase forms homodimers in solution with each of the two individual subunits comprising an FAD-binding domain, an NADPH-binding domain and an interface domain.^[1]^[2] Examples of trypanothione reducatse inhibitors include 5-Nitro-Imidazole,^[3] Febrifugine,^[4] Imipramine ^[5] and Benzoxaborole.^[6]

References

1. ^{{Cite journal|last=Bond|first=Charles S|last2=Zhang|first2=Yihong|last3=Berriman|first3=Matthew|last4=Cunningham|first4=Mark L|last5=Fairlamb|first5=Alan H|last6=Hunter|first6=William N|title=Crystal structure of Trypanosoma cruzi trypanothione reductase in complex with trypanothione, and the structure-based discovery of new natural product inhibitors|journal=Structure|volume=7|issue=1|pages=81–89|doi=10.1016/s0969-2126(99)80011-2|year=1999}}
2. ^{{Cite journal|last=Jones|first=Deuan C.|last2=Ariza|first2=Antonio|last3=Chow|first3=Wing-Huen A.|last4=Oza|first4=Sandra L.|last5=Fairlamb|first5=Alan H.|date=2010-01-01|title=Comparative structural, kinetic and inhibitor studies of Trypanosoma brucei trypanothione reductase with T. cruzi|url=http://www.sciencedirect.com/science/article/pii/S0166685109002175|journal=Molecular and Biochemical Parasitology|volume=169|issue=1|pages=12–19|doi=10.1016/j.molbiopara.2009.09.002|pmc=2789240|pmid=19747949}}
3. ^{{cite journal |vauthors=Pandey RK, Sharma D, Bhatt TK, Sundar S, Prajapati VK |title=Developing imidazole analogues as potential inhibitor for Leishmania donovani trypanothione reductase: virtual screening, molecular docking, dynamics and ADMET approach |journal= Journal of Biomolecular Structure and Dynamics|volume=33 |issue=12 |pages=2541–53 |year=2015 |pmid=26305585 |doi=10.1080/07391102.2015.1085904 }}
4. ^{{cite journal |vauthors=Pandey RK, Kumbhar BV, Srivastava S, Malik R, Sundar S, Kunwar A, Prajapati VK |title=Febrifugine analogues as Leishmania donovani trypanothione reductase inhibitors: binding energy analysis assisted by molecular docking, ADMET and molecular dynamics simulation |journal= Journal of Biomolecular Structure and Dynamics|volume=35 |issue=1 |pages=141–158 |year=2017 |pmid=27043972 |doi=10.1080/07391102.2015.1135298 }}
5. ^{{cite journal |vauthors=Pandey RK, Verma P, Sharma D, Bhatt TK, Sundar S, Prajapati VK |title=High-throughput virtual screening and quantum mechanics approach to develop imipramine analogues as leads against trypanothione reductase of leishmania |journal= Biomedicine & Pharmacotherapy|volume=83|pages= 141–152|year=2016 |pmid=27470561|doi=10.1016/j.biopha.2016.06.010 |url=http://www.sciencedirect.com/science/article/pii/S0753332216303821}}
6. ^{{cite journal |vauthors=Pandey RK, Kumbhar BV, Sundar S, Kunwar A, Prajapati VK |title=Structure-based virtual screening, molecular docking, ADMET and molecular simulations to develop benzoxaborole analogs as potential inhibitor against Leishmania donovani trypanothione reductase |journal= Journal of Receptors and Signal Transduction|volume=37 |issue=1 |pages=60–70|year=2017 |pmid=27147242|doi=10.3109/10799893.2016.1171344 }}