Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1783, Issue 4, Pages 557-566Publisher
ELSEVIER
DOI: 10.1016/j.bbamcr.2007.11.009
Keywords
sulfhydryl oxidase; Erv1; Erv2; augmenter of liver regeneration; disulfide bond; dithiol/disulfide exchange; crystal structure
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The Erv flavoenzymes contain a compact module that catalyzes the pairing of cysteine thiols into disulfide bonds. High-resolution structures of plant, animal, and fungal Erv enzymes that function in different contexts and intracellular compartments have been determined. Structural features can be correlated with biochemical properties, revealing how core sulfhydryl oxidase activity has been tailored to various functional niches. The introduction of disulfides into cysteine-containing substrates by Erv sulfhydryl oxidases is compared with the mechanisms used by NADPH-driven disulfide reductases and thioredoxin-like oxidoreductases to reduce and transfer disulfides, respectively. (C) 2007 Elsevier B.V. All rights reserved.
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