作者: W. Manieri , L. Franchini , L. Raeber , S. Dai , A.-L. Stritt-Etter
DOI: 10.1016/S0014-5793(03)00811-1
关键词:
摘要: The variable subunit of spinach ferredoxin:thioredoxin reductase (FTR) has an extended N-terminus compared to FTRs from other sources and this was proposed contribute the instability protein. We constructed two N-terminal truncation mutants recombinant FTR by removing 16 or 24 residues subunit. mutant proteins are readily expressed show half-saturation values (S(0.5)) for ferredoxin thioredoxin f comparable WT. However, increases significantly their stability. Using stabilized exposed Cys on its contact surface could be substituted without altering properties, whereas replacement active site Ser completely destabilized