Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate.
1. The activities of protein disulphide-isomerase (PDI) and thioredoxin in catalysing disulphide bond isomerization in a protein substrate were compared by using the standard assay, namely the re-activation of 'scrambled' RNAase. 2. The specific activity of PDI was 25-fold greater than that of thioredoxin. 3. The greater efficiency of PDI compared with thioredoxin is considered to be due more to the presence of multiple catalytic domains in PDI than to differences in their active-site sequences. 4. Data and procedures were defined for expressing enzyme activity in standard units, i.e. mumol of active RNAase generated/min.
Hawkins
H C
HC
Biological Laboratory, University of Kent, Canterbury, UK.
Blackburn
E C
EC
Freedman
R B
RB
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004220:Disulfides / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D007535:Isomerases / Q000378:metabolism*; D007536:Isomerism; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D019704:Protein Disulfide-Isomerases; D012260:Ribonucleases / Q000378:metabolism*; D013879:Thioredoxins / Q000378:metabolism*
D004220:Disulfides; D013879:Thioredoxins; D012260:Ribonucleases; D007535:Isomerases; D019704:Protein Disulfide-Isomerases