Note_DisulfideBonds – DisulfideBonds

WID Note_DisulfideBonds
Name DisulfideBonds
Comments Disulfide bonds reconstructed by a combination 1) primary literature, 2) homology to observed disulfide bonds [PUB_0096], and 3) computational prediction for all proteins using DiANNA v1.1 software [PUB_0299]. Cytoplasm is a reducing environment, thus few disulfide bonds form there [PUB_0300]. Periplasm and extracellular space are not reducing environments, and disulfide bonds are more commonly found there [PUB_0300]. In eukaryotes disulfide bonds are introduced by the chaperone protein disulfide isomerase (PDI) in the endoplasmic reticulum [PUB_0300]. Spontaneous disulfide bond formation is slow and error-prone [PUB_0300]. E. coli has a periplasmic enzyme (dsbA, b1185) with similar properties to PDI [PUB_0300]. M. genitalium has no dsbA ortholog. dsbA is not an essential gene [PUB_0300]. Disulfide bonds have been observed in M. fermentans P29 adhesin [PUB_0301] and M. pneumoniae OsmC [PUB_0302]. Thioredoxin plays a role in reducing disulfide bonds [PUB_0304]. TrxB mutants display additional cytoplasmic disulfide bonds [PUB_0145]. Formation of disulfide bonds in exported proteins occurs only during or after their export from the cytoplasm [PUB_0145]. Oxidized thioredoxin is not believed to contribute to disulfide bond formation [PUB_0145].
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  6. ... 2 more

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  8. UniProt Consortium. The Universal Protein Resource (UniProt) 2009. Nucleic Acids Res 37, D169-74 (2009). WholeCell: PUB_0096, PubMed: 18836194, URL:

Created 2012-10-01 15:07:34
Last updated 2012-10-01 15:13:57