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• W2005060969 abstract "Quiescin sulfhydryl oxidase (QSOX) flavoenzymes catalyze the direct, facile, insertion of disulfide bonds into reduced unfolded proteins with the reduction of oxygen to hydrogen peroxide. To date, only QSOXs from vertebrates have been characterized enzymatically. These metazoan sulfhydryl oxidases have four recognizable domains: a redox-active thioredoxin (Trx) domain containing the first of three CxxC motifs (CI−CII), a second Trx domain with no obvious redox-active disulfide, a helix-rich domain, and then an Erv/ALR domain. This last domain contains the FAD moiety, a proximal CIII−CIV disulfide, and a third CxxC of unknown function (CV−CVI). Plant and protist QSOXs lack the second Trx domain but otherwise appear to contain the same complement of redox centers. This work presents the first characterization of a single-Trx QSOX. Trypanosoma brucei QSOX was expressed in Escherichia coli using a synthetic gene and found to be a stable, monomeric, FAD-containing protein. Although evidently lacking an entire domain, TbQSOX shows catalytic activity and substrate specificity similar to the vertebrate QSOXs examined previously. Unfolded reduced proteins are more than 200-fold more effective substrates on a per thiol basis than glutathione and some 10-fold better than the parasite bisglutathione analogue, trypanothione. These data are consistent with a role for the protist QSOX in oxidative protein folding. Site-directed mutagenesis of each of the six cysteine residues (to serines) shows that the CxxC motif in the single-Trx domain is crucial for efficient catalysis of the oxidation of both reduced RNase and the model substrate dithiothreitol. As expected, the proximal disulfide CIII−CIV, which interacts with the flavin, is catalytically crucial. However, as observed with human QSOX1, the third CxxC motif shows no obvious catalytic role during the in vitro oxidation of reduced RNase or dithiothreitol. Pre-steady-state kinetics demonstrates that turnover in TbQSOX is limited by an internal redox step leading to 2-electron reduction of the FAD cofactor. In sum, the single-Trx domain QSOX studied here shows a striking similarity in enzymatic behavior to its double-Trx metazoan counterparts." @default.
• W2005060969 created "2016-06-24" @default.
• W2005060969 creator A5013915309 @default.
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• W2005060969 date "2010-02-09" @default.
• W2005060969 modified "2023-09-27" @default.
• W2005060969 title "Quiescin Sulfhydryl Oxidase from <i>Trypanosoma brucei</i>: Catalytic Activity and Mechanism of a QSOX Family Member with a Single Thioredoxin Domain" @default.
• W2005060969 cites W10600162 @default.
• W2005060969 cites W1513416677 @default.
• W2005060969 cites W1532244484 @default.
• W2005060969 cites W1549766496 @default.
• W2005060969 cites W1590299690 @default.
• W2005060969 cites W1717942436 @default.
• W2005060969 cites W1972119798 @default.
• W2005060969 cites W1974016096 @default.
• W2005060969 cites W1975155762 @default.
• W2005060969 cites W1975384954 @default.
• W2005060969 cites W1979484538 @default.
• W2005060969 cites W1982616392 @default.
• W2005060969 cites W1985339378 @default.
• W2005060969 cites W1985616824 @default.
• W2005060969 cites W1989719739 @default.
• W2005060969 cites W1990146329 @default.
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• W2005060969 cites W2007979078 @default.
• W2005060969 cites W2008807736 @default.
• W2005060969 cites W2012061626 @default.
• W2005060969 cites W2013783645 @default.
• W2005060969 cites W2016121977 @default.
• W2005060969 cites W2017400110 @default.
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• W2005060969 cites W2023356380 @default.
• W2005060969 cites W2024071324 @default.
• W2005060969 cites W2029112137 @default.
• W2005060969 cites W2030145012 @default.
• W2005060969 cites W2031894797 @default.
• W2005060969 cites W2037576269 @default.
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• W2005060969 cites W2040652684 @default.
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• W2005060969 cites W2047138766 @default.
• W2005060969 cites W2047763620 @default.
• W2005060969 cites W2048753887 @default.
• W2005060969 cites W2051008192 @default.
• W2005060969 cites W2063963880 @default.
• W2005060969 cites W2072479668 @default.
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• W2005060969 cites W2080533036 @default.
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• W2005060969 doi "https://doi.org/10.1021/bi902222s" @default.
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