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1.8.1.6: cystine reductase

This is an abbreviated version!
For detailed information about cystine reductase, go to the full flat file.

Word Map on EC 1.8.1.6

Reaction

2 L-cysteine +

NAD+
=
L-cystine
 +
NADH
 +
H+

Synonyms

CydDC, CysR, cystine reductase (NADH), cystine reductase (NADH2), EC 1.6.4.1, L-cysteine:NAD+ oxidoreductase, L-cystine reductase, NADH-dependent cystine reductase, NADH2:L-cystine oxidoreductase, reductase, cystine, thioredoxin domain containing 17, thioredoxin-like 5, TRP14, TXNDC17, TXNL5

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.1 With NAD+ or NADP+ as acceptor
                1.8.1.6 cystine reductase

General Information

General Information on EC 1.8.1.6 - cystine reductase

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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
metabolism
-
the enzyme complex CydDC does not export L-cysteine from cytoplasm, but rather reduces cytoplasmic cystine
physiological function
-
the enzyme sensitizes Escherichia coli to oxidative (H2O2) stress and aminoglycosides
additional information