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• W2067200555 abstract "TlpA, the membrane‐anchored, thioredoxin‐like protein from Bradyrhizobium japonicum , is essential for cytochrome aa 3 biogenesis. The periplasmic domain of TlpA was previously shown to have protein thiol:disulfide oxidoreductase activity and reducing properties similar to those of cytoplasmic thioredoxins. Here, we replaced the proline‐109 in its active‐site sequence C 107 V 108 P 109 C 110 by a histidine residue. The resulting active‐site motif (CVHC) resembles that of oxidizing thiol:disulfide oxidoreductases such as protein disulfide isomerase (PDI) and DsbA. Indeed, the TlpA variant P109H was by 66 mV more oxidizing than the wild‐type protein. Nevertheless, the altered protein was even more efficient in catalyzing the reduction of insulin disulfides by dithiothreitol than the wild‐type due to a faster recycling of its catalytically active, reduced form. Cells of B. japonicum expressing only the mutated tlpA gene had the same phenotypes as wild‐type cells, suggesting that the change in the redox potential of TlpA was not critical for its in vivo function." @default.
• W2067200555 created "2016-06-24" @default.
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• W2067200555 date "1997-04-14" @default.
• W2067200555 modified "2023-10-17" @default.
• W2067200555 title "Replacement of Pro¹⁰⁹ by His in TlpA, a thioredoxin‐like protein from <i>Bradyrhizobium japonicum</i>, alters its redox properties but not its in vivo functions" @default.
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• W2067200555 doi "https://doi.org/10.1016/s0014-5793(97)00270-6" @default.
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