Table 3.

Properties of active-site variants of protein disulfide isomerase.

PDIa	Dithiol oxidation activityb	Disulfide reduction activityc	Disulfide isomerization activityd	Doubling time of complemented pdi1Δ S. cerevisiaee
CGHC	100	100	100	1.8 ± 0.2
CGHS	3	6	93	2.3 ± 0.6
SGHC	0	3	4	NC

Data from ref (49).

NC, no complementation.

^aFor each protein, the sequence indicated is present in both active sites of rat PDI.

^bPercentage of wild-type PDI activity for the activation of reduced RNase A.

^cPercentage of wild-type PDI activity for the reduction of the disulfide bonds in insulin.

^dPercentage of wild-type PDI activity for the activation of scrambled RNase A.

^eRelative to cells complemented with S. cerevisiae PDI.