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. Author manuscript; available in PMC: 2020 Dec 23.
Published in final edited form as: Chem Biol Interact. 2019 Jul 17;310:108756. doi: 10.1016/j.cbi.2019.108756

Table 2.

Kinetic parameters determined for ATC and BTC

Enzyme Substrate kcat
(min−1)
KM
(μM)
kcat/KM
(min−1 M−1)
RCEc Kss
(μM)
b
hBChE-7a BTC 46715 30.0 ± 2.5 1.56 × 109 0.74 1291 2.80
hBChE b BTC 29500 ± 1100 14.0 ± 1.8 2.11 × 109 1.00 3010d 3.36
BChE-M47 BTC 355 ± 1300 24.8 ± 3.3 1.43 × 109 0.68 4983 2.99
BChE-M48 BTC 334 ± 1030 28.5 ± 3.1 1.17 × 109 0.55 6760 3.11
hBChE b ATC 20200 ± 910 57.0 ± 6.4 3.54 × 108 1.00 2890 2.47
BChE-M47 ATC 19960 ± 830 38.5 ± 4.5 5.18 × 108 1.46 5000 3.03
BChE-M48 ATC 17270 ± 640 41.9 ±5.3 4.12 × 108 1.16 4310 2.62
a

The kcat, KM, Kss, and b for hBChE-7 against BTC came from reference [32].

b

The kcat and KM for BChE expressed in CHO cells (hBChE) against BTC and ATC, Kss and b for hBChE against ATC came from in reference [49].

c

RCE refers to the relative catalytic efficiency (kcat/KM), i.e. the ratio of (kcat/KM) of the different BChE mutants against the same substrate.

d

The Kss and b for hBChE against BTC came from reference[50].