Catalysis of Oxidative Protein Folding by Mutants of Protein Disulfide Isomerase with a Single Active-Site Cysteine

Protein disulfide isomerase (PDI), a very abundant protein in the endoplasmic reticulum, facilitates the formation and rearrangement of disulfide bonds using two nonequivalent redox active-sites, located in two different thioredoxin homology domains [Lyles, M. M., & Gilbert, H. F. (1994) J. Biol...

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Veröffentlicht in:	Biochemistry (Easton) 1996-02, Vol.35 (6), p.1972-1980
Hauptverfasser:	Walker, Kenneth W, Lyles, Michelle M, Gilbert, Hiram F
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Base Sequence Binding Sites - genetics Catalysis Cattle Cysteine - chemistry Disulfides - chemistry DNA Primers - genetics In Vitro Techniques Isomerases - chemistry Isomerases - genetics Isomerases - metabolism Kinetics Models, Chemical Molecular Sequence Data Mutagenesis, Site-Directed Oxidation-Reduction Point Mutation Protein Disulfide-Isomerases Protein Folding Rats Ribonucleases - chemistry Ribonucleases - metabolism
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