Table 2 Kinetic parameters of Ac-SDKP hydrolysis by different ACE enzymes.

From: Structural basis of Ac-SDKP hydrolysis by Angiotensin-I converting enzyme

Enzyme

kcat (s−1)

Km (μM)

kcat/Km (s−1.M−1)

N-dom

14.2 ± 1.2

199.6 ± 25.5

(0.72 ± 0.06) × 105

C-dom

4.8 ± 0.6

138.2 ± 20.3

(0.35 ± 0.01) × 105

sACE

12.7 ± 0.4

239.5 ± 29.4

(0.54 ± 0.06) × 105

N-sACE

34.0 ± 3.9

493.8 ± 79.3

(0.70 ± 0.04) × 105

C-sACE

8.2 ± 0.5

436.3 ± 33.4

(0.188 ± 0.002) × 105

CC-sACE

19.4 ± 0.8

503.8 ± 31.6

(0.39 ± 0.03) × 105

  1. Turnover rates were normalised to activity per unit active site for enzymes containing two functional domains (sACE and CC-sACE).