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EC Number General Information Commentary Reference
Show all pathways known for 1.8.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.6evolution the enzyme belongs to the member of the thioredoxin (Trx)-fold protein family. The enzyme lacks activity with classical thioredoxin, Trx1, substrates. Human enzyme TRP14 has high enzymatic activity in reduction of L-cystine, where the catalytic efficiency coupled to Trx reductase 1 (TrxR1) using NADPH is fivefold higher than the activity of enzyme Trx1 alone. Trx1-mediated L-cystine reduction is inefficient in the presence of other preferred Trx1 substrates whereas, conversely, TRP14 seems to be a more dedicated L-cystine reductase 743682
Show all pathways known for 1.8.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.6metabolism the enzyme complex CydDC does not export L-cysteine from cytoplasm, but rather reduces cytoplasmic cystine 765683
Show all pathways known for 1.8.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.6more the disulfide/dithiol motif formed by Cys43 and Cys46 is the active site of TRP14 743682
Show all pathways known for 1.8.1.6Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.6physiological function the enzyme sensitizes Escherichia coli to oxidative (H2O2) stress and aminoglycosides 765683
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