A proposed reaction mechanism for rice NADPH thioredoxin reductase C, an enzyme with protein disulfide reductase activity |
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Authors: | Juan Manuel Pérez-Ruiz |
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Institution: | Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla and CSIC, Avda Américo Vespucio 49, 41092 Sevilla, Spain |
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Abstract: | NADPH thioredoxin reductase C (NTRC) is an interesting NTR with a thioredoxin (Trx) domain at the C-terminus, able to conjugate both activities for 2-Cys peroxiredoxin (Prx) reduction. NTRC is dimeric in the presence of NADPH and interacted with dimeric 2-Cys Prx through the Trx module by a mixed disulfide between Cys377 of NTRC and Cys61 of the 2-Cys Prx. NTRC variants of both NTR and Trx active sites were inactive, but 1:1 mixtures of both variants allowed partial recovery of activity suggesting inter-subunit transfer of electrons during catalysis. Based on these results we propose a model for the reaction mechanism of NTRC.Structured summaryMINT-7017333: 2cys Prx (uniprotkb:Q6ER94) and 2cys Prx (uniprotkb:Q6ER94) bind (MI:0407) by molecular sieving (MI:0071)MINT-7017101, MINT-7017183: NTRC (uniprotkb:Q70G58) and 2cys Prx (uniprotkb:Q6ER94) bind (MI:0407) by enzymatic studies (MI:0415) |
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Keywords: | NTR NADPH thioredoxin reductase Prx peroxiredoxin Trx thioredoxin |
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