Structural basis for a distinct catalytic mechanism in Trypanosoma brucei tryparedoxin peroxidase

J Melchers, M Diechtierow, K Fehér, I Sinning… - Journal of Biological …, 2008 - ASBMB
Trypanosoma brucei, the causative agent of African sleeping sickness, encodes three
cysteine homologues (Px I-III) of classical selenocysteine-containing glutathione
peroxidases. The enzymes obtain their reducing equivalents from the unique trypanothione
(bis (glutathionyl) spermidine)/tryparedoxin system. During catalysis, these tryparedoxin
peroxidases cycle between an oxidized form with an intramolecular disulfide bond between
Cys 47 and Cys 95 and the reduced peroxidase with both residues in the thiol state. Here …

Structural basis for a distinct catalytic mechanism in Trypanosoma brucei tryparedoxin peroxidase.

J Melchers, M Diechtierow, K Fehér, I Sinning… - Journal of Biological …, 2011 - ASBMB
In the left column, the sentence beginning on line 12 from the bottom should read as
follows:“In addition, the wild type enzyme obtained here exerted a three times higher specific
activity.” The sentence beginning on line 5 from the bottom should read as follows:“The
apparent second order rate constants (k1) of wild type, Glu97, and Glu99 Px III were on the
same order of magnitude, whereas the k2 values of Glu97 and Glu99 Px III were 10 and 5
times lower than that of the wild type enzyme, respectively (Table 3).” The corrected version …
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