A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease.

Abstract excerpt

Thioredoxin (Trx) from Escherichia coli was compared with bovine protein disulfide-isomerase (PDI) for its ability to catalyze native disulfide formation in either reduced or randomly oxidized (scrambled) ribonuclease A (RNase). On a molar basis, a 100-fold higher concentration of Trx than of PDI was required to give the same rate of native disulfide formation measured as recovery of RNase activity. A Pro-34 to...

Topics

• Amino Acid Sequence
• Animals
• Binding Sites
• Catalysis
• Cattle
• Escherichia coli
• Histidine
• Isomerases
• Kinetics
• Molecular Sequence Data
• Mutation