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. Author manuscript; available in PMC: 2016 Mar 1.
Published in final edited form as: Biochem J. 2015 Mar 1;466(2):243–251. doi: 10.1042/BJ20141266

Table 1.

Kinetic parameters determined for (−)-cocaine, ACh, and BTC hydrolyses catalyzed by mBChE, mCocH, hBChE, and hCocH.

Enzyme Substrate kcat
(min−1)		 KM
(µM)		 kcat/KM
(min−1 M−1)		 RCEa Kss
(µM)		 b
mBChE (−)-cocaine 1.4 1.6 8.8 × 105 1 1300 3.13
mCocH (−)-cocaine 250 35 7.1 × 106 8.2 1500 0.88
hBChEb (−)-cocaine 4.1 4.5 9.1 × 105 1 216 1.80
hCocHc (−)-cocaine 5700 3.1 1.8 × 109 2020 137 0.40
mBChE ACh 38400 400 9.6× 107 1 15200 1.79
mCocH ACh 19000 210 9.0 × 107 0.94 25800 0.30
hBChEd ACh 61200 148 4.1 × 108 1 31600 2.58
hCocHe ACh 11900 37 3.2 × 108 0.78 30000 0.68
mBChE BTC 35600 72 4.9 × 108 1 5000 2.77
mCocH BTC 28200 99 2.8 × 108 0.58 254 0.19
hBChEf BTC 29500 17 1.7 × 109 1 3010 3.36
hCocHe BTC 28000 13 2.2 × 109 1.24 243 0.49
a

RCE refers to the relative catalytic efficiency (kcat/KM), i.e. the ratio of the kcat/KM value of a mutant (mCocH or hCocH) to that of the corresponding wild-type enzyme (mBChE or hBChE) against the same substrate.

b

The kcat and KM for hBChE against (−)-cocaine were reported in ref.([8]).

c

The kcat and KM for hCocH against (−)-cocaine were reported in ref.([16]).

d

The kcat and KM for hBChE against ACh were reported in ref.([50]).

e

The kcat and KM for hCocH against ACh and BTC were reported in ref.([51]).

f

The kcat and KM for hBChE against BTC were reported in ref.([20]).