Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm.
Disulfide bond formation is a catalyzed process in vivo. In prokaryotes, the oxidation of cysteine pairs is achieved by the transfer of disulfides from the highly oxidizing DsbA/DsbB catalytic machinery to substrate proteins. The oxidizing power utilized by this system comes from the membrane-embedded electron transport system, which utilizes molecular oxygen as a final oxidant. Proofreading of disulfide bond formation is performed by the DsbC/DsbD system, which has the ability to rearrange non-native disulfides to their native configuration. These disulfide isomerization reactions are sustained by a constant supply of reducing power provided by the cytoplasmic thioredoxin system, utilizing NADPH as the ultimate electron source.
Nakamoto
Hitoshi
H
Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830, North University Dr., Ann Arbor, MI 48109-1048, USA.
Bardwell
James C A
JC
D002384:Catalysis; D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D004220:Disulfides / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D019897:Periplasm / Q000201:enzymology* / Q000378:metabolism; D019704:Protein Disulfide-Isomerases / Q000378:metabolism*; D015202:Protein Engineering; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D004220:Disulfides; D011994:Recombinant Proteins; D019704:Protein Disulfide-Isomerases; D003545:Cysteine