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Biochim Biophys Acta. 2008 Apr;1783(4):557-66. Epub 2007 Nov 29.

The Erv family of sulfhydryl oxidases.

Author information

1
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel. deborah.fass@weizmann.ac.il

Abstract

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.

PMID:
18155671
DOI:
10.1016/j.bbamcr.2007.11.009
[Indexed for MEDLINE]
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