. Author manuscript; available in PMC: 2014 Feb 26.

Published in final edited form as: Biochemistry. 2013 Feb 14;52(8):1364–1372. doi: 10.1021/bi400013k

Table 3. Relative activity of wild type and mutant Ath α-DOX constructs.

Oxygenase activity was measured with 10μg of protein construct and 200μM LA as the substrate using an oxygen electrode as described under “Experimental Procedures”. A value of 100% is assigned for the oxygenase activity of wild-type Ath α-DOX, with mutant activity normalized to the wild-type construct. Values represent the average of 3 trials. Values for Osa α-DOX are from (9). The residue numbering equivalences between Ath and Osa α-DOX are as follows: Q159:Q153; H318:H311; T323:T316; Y386:Y379; R565:R558; R566:R559. ND, not determined.

Construct	Relative Activity (%)
Construct	Ath α-DOX	Osa α-DOX

wild type	100	100
Q159N	85.5	ND
Q159S	100	ND
Q159V	75.4	ND
H318A	6.9	2.6
H318Q	25.3	11.5
T323A	7.0	ND
T323L	0.0	ND
Y386F	0.0	0.0
R565A	76.0	46.7
R565K	32.0	18.4
R565L	55.0	74.2
R566A	0.0	0.4
R566K	2.8	0.9
R566L	0.0	0.0