期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
卷 1783, 期 4, 页码 567-577出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2007.10.002
关键词
sulfhydryl oxidase; QSOX; oxidative protein folding; disulfide exchange; protein disulfide isomerase
资金
- NIGMS NIH HHS [T32 GM008550, R01 GM026643-29, T32GM08550, GM26643, R01 GM026643] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM008550, R01GM026643] Funding Source: NIH RePORTER
The Quiescin-sulfhydryl oxidase (QSOX) family of flavoenzymes catalyzes the direct and facile insertion of disulfide bonds into unfolded reduced proteins with concomitant reduction of oxygen to hydrogen peroxide. This review discusses the chemical mechanism of these enzymes and the involvement of thioredoxin and flavin-binding domains in catalysis. The variability of CxxC motifs in the QSOX family is highlighted and attention is drawn to the steric factors that may promote efficient thiol/disulfide exchange during oxidative protein folding. The varied cellular location of these multi-domain sulfhydryl oxidases is reviewed and potential intracellular and extracellular roles are summarized. Finally, this review identifies important unresolved questions concerning this ancient family of sulfhydryl oxidases. (C) 2007 Elsevier B.V. All rights reserved.
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