Disulfide bond isomerization in prokaryotes.
Proteins with multiple cysteine residues often require disulfide isomerization reactions before they attain their correct conformation. In prokaryotes this reaction is catalyzed mainly by DsbC, a protein that shares many similarities in structure and mechanism to the eukaryotic protein disulfide isomerase. This review discusses the current knowledge about disulfide isomerization in prokaryotes.
Gleiter
Stefan
S
Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI 48109-1048, USA.
Bardwell
James C A
JC
D000818:Animals; D004220:Disulfides / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D007536:Isomerism; D011387:Prokaryotic Cells / Q000201:enzymology*; D011487:Protein Conformation; D019704:Protein Disulfide-Isomerases / Q000737:chemistry* / Q000502:physiology
D004220:Disulfides; D019704:Protein Disulfide-Isomerases