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. 2012 Sep 25;7(9):e45949. doi: 10.1371/journal.pone.0045949

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.