. Author manuscript; available in PMC: 2009 Jun 1.

Published in final edited form as: Protein Expr Purif. 2008 Mar 10;59(2):349–356. doi: 10.1016/j.pep.2008.03.002

Table 3.

Comparison of steady state kinetic parameters for recombinant human and rat liver MAOBs expressed in P. pastoris. The k_cat and K_m (Benzylamine) values are determined at an [O₂] of 0.24 mM.

	Recombinant human liver^a	Recombinant rat liver
Benzylamine
K_m (amine) mM	0.15 ± 0.01	0.176 ± 0.015
k_cat min⁻¹	300 ± 10	497 ± 83
K_m (O₂) mM	0.33 ± 0.07	0.17 ± 0.01
[α, α -²H₂]Benzylamine
K_m (amine) mM	0.146 ± 0.01	0.26 ± 0.02
k_cat min⁻¹	64 ± 5	149 ± 24
K_m (O₂) mM	0.074 ± 0.023	0.03 ± 0.006
Deuterium isotope effect
^Dk_cat	4.7 ± 0.5	3.4 ± 0.7
^D[k_cat/K_m(amine)]	4.6 ± 0.46	4.9 ± 0.4
^D[k_cat/K_m(O₂)]	1.0 ± 0.34	0.62 ± 0.14
Apparent K_d (µM)	147 ± 25	304 ± 84

The values for the human enzyme are calculated from the values listed in Ref. [13].