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. 2011 Apr 13;286(23):20736–20745. doi: 10.1074/jbc.M111.230367

TABLE 2.

Oxygenation of AA, 1-AG, and 2-AG by wild type and mutant constructs of muCOX-2

Oxygen consumption was measured using an oxygen electrode as described under “Experimental Procedures.” kcat and Km values were derived from triplicate measurements, utilizing 5 μg of protein in the electrode chamber. E, efficiency, defined as kcat/Km; ND, not determined.

Construct AA
2-AG
1-AG
kcat Km E kcat Km E kcat Km E
s1 μm s1 μm s1 μm
Wild-type 27.0 ± 0.4 5.1 ± 0.3 5.2 23.7 ± 1.7 8.5 ± 1.6 2.8 19.7 ± 1.0 7.3 ± 1.1 2.7
Y355F 15.0 ± 0.3 12.3 ± 0.8 1.2 23.8 ± 0.7 2.7 ± 0.3 8.8 ND ND ND
R513H 28.7 ± 0.5 11.0 ± 0.6 2.6 19.7 ± 0.9 7.2 ± 1.0 2.7 19.1 ± 0.8 9.1 ± 1.1 2.1
L531Aa 13.9 ± 0.3 3.7 ± 0.3 3.8 14.9 ± 0.4 4.4 ± 0.4 3.4 ND ND ND
L531F 23.3 ± 0.4 14.9 ± 0.8 1.6 18.9 ± 0.6 7.3 ± 0.8 2.6 19.5 ± 0.6 7.1 ± 0.6 2.7
L531P 14.9 ± 0.3 2.9 ± 0.3 5.1 16.3 ± 0.9 8.2 ± 1.2 2.0 ND ND ND

a Kinetic parameters for the oxygenation of AA by wild-type enzyme, as well as L531A and L531P mutant constructs, are from Ref. 10.