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JBC, Vol. 254, Issue 19, 9627-9632, Oct, 1979
A. Holmgren
Thioredoxin from Escherichia coli was shown to catalyze the reduction of
insulin disulfides by dithiothreitol. A quantitative assay was developed
which measures the rate of insulin reduction spectrophotometrically at 650
nm as turbidity formation from the precipitation of the free insulin B
chain. Thioredoxin, at 5 microM concentration, accelerated the reaction
between 0.130 mM insulin and 1.0 mM dithiothreitol at pH 7 around 20-fold.
The pH optimum of the reaction was 7.5. Thioredoxins from E. coli and calf
liver showed similar specific activities. Stopped flow fluorescence
measurements of the rate of reduction of thioredoxin-S2 by dithiothreitol
showed a second order rate constant of 1647 M-1 s-1 at pH 7.2. This is
between 10(2) to 10(3) times larger than the reaction between insulin or
linear model disulfides and dithiothreitol. It is consistent with a
ping-pong mechanism of thioredoxin catalysis since reduced thioredoxin is
known to react very fast with insulin. Thioredoxin also catalyzed
lipoamide-dependent reduction of the insulin disulfides in a coupled system
with NADH, lipoamide, and lipoamide dehydrogenase. The fast spontaneous
reaction between dihydrolipoamide and thioredoxin-S2 provides a mechanism
for NADH or pyruvate-dependent disulfide reduction. The implication of the
dithiol-disulfide oxidoreductase activity of thioredoxin for the regulation
of enzyme activities by thiol oxidation-reduction control is discussed.
Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
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V. G. Panse, P. Vogel, W. E. Trommer, and R. Varad |
