. 2009 Feb 23;9:12. doi: 10.1186/1472-6750-9-12

Table 1.

Catalytic parameters and expression levels of wild-type and CotA mutants.

Enzyme variant	K_M(μM)^a	Specific activity (μmol min^-1mg^-1)^a	Catalytic efficiency (μmol min^-1mg^-1μM^-1)	Volumetric activity (U l^-1)^a	Protein yield (mg l^-1)^b	Improvement factor
CotA	6.5 ± 0.2	16.0 ± 0.2	2.46	410 ± 10	26	1
D500G	9.5 ± 0.2	11.1 ± 0.1	1.17	2200 ± 200	199	7.8
K316N	10.0 ± 0.3	14.0 ± 0.2	1.40	1100 ± 100	79	3.1
K316N/D500G	8.4 ± 0.2	11.7 ± 0.2	1.39	3400 ± 100	291	11.4

^aDetermined using ABTS as substrate in 0.1 M citrate/phosphate buffer, pH 4.0. Each value was calculated from three independent experiments.

^bCalculated on the basis of volumetric activity and specific activity of each laccase variant.