Disulfide bond isomerization in prokaryotes
نویسندگان
چکیده
منابع مشابه
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.
متن کاملCatalysis of protein disulfide bond isomerization in a homogeneous substrate.
Protein disulfide isomerase (PDI) catalyzes the rearrangement of nonnative disulfide bonds in the endoplasmic reticulum of eukaryotic cells, a process that often limits the rate at which polypeptide chains fold into a native protein conformation. The mechanism of the reaction catalyzed by PDI is unclear. In assays involving protein substrates, the reaction appears to involve the complete reduct...
متن کاملElectron Avenue Pathways of Disulfide Bond Formation and Isomerization
extracytoplasmic environments (e.g., the lumen of the eukaryotic endoplasmic reticulum and the gram-negative bacterial periplasmic space). In contrast, the cytoplasm displays a network of enzymes and molecules dedicated to the reduction of disulfide bonds (Åslund Laurent Debarbieux and Jon Beckwith* Department of Microbiology and Molecular Genetics Harvard Medical School Boston, Massachusetts 0...
متن کاملCatalysis 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...
متن کاملSynthesis of Zinc Dimethyldithiocarbamate by Reductive Disulfide Bond Cleavage of Tetramethylthiuram Disulfide in Presence of Zn2+
The zinc(II) complex [Zn2(dmdtc)2(μ-dmdtc)2] has been synthesized directly from thiram ligand, containing a disulfide bond {dmdtc = N,N-dimethyldithiocarbamate; thiram = N,N-tetramethylthiuram disulfide}, and characterized by elemental analysis and spectroscopic methods. Surprisingly thiram, undergoes a reductive disulfide bond scission upon reaction with Zn2+ in methanolic media to give the [Z...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
سال: 2008
ISSN: 0167-4889
DOI: 10.1016/j.bbamcr.2008.02.009