Evidence for the co‐existence of glutathione reductase and trypanothione reductase in the non‐trypanosomatid Euglenozoa: Euglena gracilis Z

FEBS Letters

Laval-Martin, Danielle L¹  Montrichard, Françoise¹  Le Guen, Fabienne¹  Davioud-Charvet, Elisabeth² 

[1] G.B.B.M.V.-EA917, UFR Sciences, 2 boulevard Lavoisier, 49045 Angers, France;Institut de Biologie-Institut Pasteur de Lille, URA CNRS 1309, Université Lille II, 1 rue du Pr. Calmette, BP 447, 59021 Lille cedex, France

关键词: Trypanothione reductase;    Glutathione reductase;    Thioredoxin reductase;    Trypanosomatid;    Euglena gracilis;    DTNB;    5;    5′-dithiobis(2-nitrobenzoate);    GR;    glutathione reductase;    GSSG;    glutathione disulfide;    Gspd(S)2;    glutathionylspermidine disulfide;    TR;    trypanothione reductase;    Trx(S)2;    thioredoxin disulfide;    TrxR;    thioredoxin reductase;    T(S)2;    trypanothione disulfide;   

DOI  :  10.1016/S0014-5793(98)01606-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two NADPH-dependent disulfide reductases, glutathione reductase and trypanothione reductase, were shown to be present in Euglena gracilis, purified to homogeneity and characterized. The glutathione reductase (M _r 50 kDa) displays a high specificity towards glutathione disulfide with a K _M of 54 μM. The amino acid sequences of two peptides derived from the trypanothione reductase (M _r 54 kDa) show a high level of identity (81% and 64%) with sequences of trypanothione reductases from trypanosomatids. The trypanothione reductase is able to efficiently reduce trypanothione disulfide (K _M 30.5 μM) and glutathionylspermidine disulfide (K _M 90.6 μM) but not glutathione disulfide, nor Escherichia coli thioredoxin disulfide, nor 5,5′-dithiobis(2-nitrobenzoate) (DTNB). These results demonstrate for the first time (i) the existence of trypanothione reductase in a non-trypanosomatid organism and (ii) the co-existence of trypanothione reductase and glutathione reductase in E. gracilis.

【 授权许可】

Unknown