. Author manuscript; available in PMC: 2012 Apr 12.

Published in final edited form as: Biochemistry. 2011 Mar 18;50(14):3025–3033. doi: 10.1021/bi101832w

Table 2. Summary of kinetic parameters for hydrolysis of N-terminal L-Asn angiotensin II (N¹-AII) by hNTAN1.

Kinetic parameters were derived from nonlinear fit of the Michaelis-Menten equation to initial rate measurements. Reactions were carried out at 37°C in 50mM Tris-HCl, 150mM NaCl, pH 7.5. The parenthetical in the enzyme column depicts whether purified hNTAN1 was expressed from pNTANFLAGSII (+ Gly2) or from pNTAN2FLAGSII (− Gly2).

Enzyme	K_M (μM)	k_cat (s⁻¹)	k_cat/K_M (M⁻¹s⁻¹)
hNTAN1 (+Gly2)	31 ± 4	2.3 ± 0.07	7.4 ± 1 × 10⁴
hNTAN1 (−Gly2)	35 ± 3	6.6 ± 0.1	1.9 ± 0.2 × 10⁵

Table 2. Summary of kinetic parameters for hydrolysis of N-terminal L-Asn angiotensin II (N1-AII) by hNTAN1.

Table 2. Summary of kinetic parameters for hydrolysis of N-terminal L-Asn angiotensin II (N¹-AII) by hNTAN1.