Table 1. Enzymatic spectra and stability parameters of WT and mutant CKs.
CKs | k m-creatine (mM) | k m-ATP (mM) | k cat (S−1) | k cat/k m -ATP (M−1S−1) | ANS intensity | E max (nm) | T m (°C) |
WT | 3.6±0.7 | 0.39±0.08 | 148±6 | 0.38±0.02 | 44.6±1.9 | 333 | 42.7±0.7 |
H26Y | 4.5±1.2 | 0.89±0.08 | 45±1 | 0.051±0.001 | 90.1±0.9 | 335 | 34.9±1.0 |
P36T | 3.9±0.1 | 0.2±0.06 | 49±5 | 0.25±0.03 | 69.1±3.0 | 334 | 32.3±0.5 |
T59I | 24.4±4.3 | 3.8±0.6 | 12±1 | 0.0032±0.0003 | 69.7±3.9 | 334 | 44.7±0.6 |
P67Q | 8.1±0.7 | 0.40±0.08 | 114±6 | 0.29±0.02 | 55.6±1.7 | 333 | 40.7±1.0 |
K177R | 3.9±0.2 | 0.33±0.07 | 111±8 | 0.34±0.02 | 63.8±3.0 | 333 | 41.6±1.3 |
K267E | 3.8±0.3 | 0.47±0.05 | 192±12 | 0.41±0.03 | 53.5±1.1 | 333 | 38.0±0.9 |
S309L | 4.8±0.4 | 0.39±0.09 | 143±7 | 0.37±0.02 | 49.4±0.4 | 333 | 42.3±0.4 |
L360F | 4.7±0.2 | 0.42±0.1 | 130±6 | 0.31±0.01 | 44.7±0.8 | 333 | 40.9±0.7 |
Data are presented as the mean ± sd (n = 3). Abnormal values are in bold.