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. 2004 Apr 7;101(16):5940–5945. doi: 10.1073/pnas.0306708101

Table 2. Steady-state activity of the covalent complex (PCXL) compared with C128A (wild-type CCP) and the V197C/C128A mutant at pH 6.

Kcat, sec-1
20 mM potassium phosphate
200 mM potassium phosphate
Enzyme Horse cyt. c Yeast cyt. c Horse cyt. c Yeast cyt. c
WT CCP 850.3 ± 51.0 (100) 219.1 ± 11.8 (100) 175.1 ± 9.5 (100) 1361.8 ± 57.4 (100)
V197C/C128A 803.4 ± 17.0 (95) 240.9 ± 7.3 (109) 166.8 ± 7.2 (95) 1167.2 ± 17.7 (86)
PCXL 20.7 ± 2.0 (2.4) 15.7 ± 0.9 (7.2) 4.2 ± 0.09 (2.4) 76.2 ± 4.2 (5.6)

The values in parentheses are percent of wild-type activity.