Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains.

Article

Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains.

The Journal of biological chemistry - 9 Dec 1994

Lyles M M, Gilbert H F

Abstract excerpt

Protein disulfide isomerase (PDI), a foldase of the endoplasmic recticulum, is a multifunctional protein that catalyzes the formation and isomerization of disulfide bonds during protein folding. The wild-type protein contains two redox active thiol/disulfide sites near the N and C terminus that a...

Topics

Amino Acid Sequence
Base Sequence
Catalysis
DNA Primers
Isomerases
Kinetics
Molecular Sequence Data
Mutation
Oxidation-Reduction
Protein Disulfide-Isomerases
Protein Folding
Ribonucleases
Thioredoxins

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