Recombinant Expression and Characterization of Human and Murine ACE2: Species-Specific Activation of the Alternative Renin-Angiotensin-System

Table 1

Enzymatic properties of rhACE2 and rmACE2. The substrate turnover rates and product formation rates were determined for the kinetic experiments in Figure 2. Therefore, the slope of the linear regressions across all data points was determined for both substrate-product pairs and both enzymes. The mean of the absolute values for the substrate degradation rates and product formation rates for each enzyme were related to the molar concentration of rhACE2 or rmACE2. The resulting values for 𝑘_cat are given in the table.

	𝑘cat [s^−1]
	rhACE2	rmACE2
Ang 1–8 ≥ Ang 1–7	7.7×10^−1	6.2×10^−1
Ang 1–10 ≥ Ang 1–9	1.8×10^−2	1.3×10^−3