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. 2013 Jun 14;8(6):e66426. doi: 10.1371/journal.pone.0066426

Table 2. Kinetic parametersa of recombinant laccases on benchmark substrates (mean ± SD).

Lcc4A Lcc5 Lcc7 Lcc1A Lcc1B
Substrate Km (µM) Vmax (U mg−1)b Vmax/Km (U mg−1 M−1)b Km (µM) Vmax (U mg−1)b Vmax/Km (U mg−1 M−1)b Km (µM) Vmax (U mg−1)b Vmax/Km (U mg−1 M−1)b Km (µM) Vmax (U mg−1)b Vmax/Km (U mg−1 M−1)b Km (µM) Vmax (U mg−1)b Vmax/Km (U mg−1 M−1)b
ABTS 11.2±0.9 0.61±0.01 (5.44±0.31)×104 325±47 2.26±0.36 (6.94±0.16) ×103 36.3±1.9 19.7±0.6 (5.43±0.23) ×105 14.3±1.9 2.65±0.65 (1.92±0.75)×105 42.5±10.3 5.61±2.26 (1.28±0.22)×105
CAT 255±76 0.91±0.11 (3.72±0.75)×103 6280±680 2.65±0.10 (4.24±0.31) ×102 38800±5300 0.53±0.05 13.8±0.08 2030±140 0.62±0.13 (3.08±0.85)×102 3540±230 0.94±0.31 (2.69±0.95)×102
DMP 26.0±2.4 0.26±0.03 (1.00±0.03)×104 113±8 0.60±0.03 (5.30±0.28) ×103 12000±1000 1.73±0.09 (1.44±0.05) ×102 120±4 1.08±0.24 (8.94±1.79)×103 115±17 1.41±0.52 (1.20±0.29)×104
DOPA 1040±150 1.07±0.10 (1.03±0.05)×103 10500±700 1.66±0.15 (1.58±0.07) ×102 n.a.c n.a. n.a. 4550±570 0.49±0.19 (1.06±0.28)×102 5520±850 0.65±0.15 (1.22±0.45)×102
GUA 648±105 0.16±0.01 (2.46±0.27)×102 1270±90 0.32±0.01 (2.57±0.17) ×102 8630±2120 0.18±0.05 21.4±0.3 943±58 0.73±0.13 (7.85±1.72)×102 913±68 0.96±0.25 (1.07±0.35)×103
SGZ n.d.d 0.09±0.01 n.d. n.d. 0.02±0.00 n.d. n.d. 2.52±0.81 n.d. n.d. 0.98±0.20 n.d. n.d. 0.75±0.07 n.d.
TYR n.a. n.a. n.a. n.a. n.a. n.a. n.a. n.a. n.a. n.a. n.a. n.a. n.a. n.a. n.a.
a

Apparent values. Parameters of Lcc1A and Lcc1B were obtained from our previous study [2].

b

One U was defined as the number of µmol of respective oxidized product formed in one minute under standard assay condition.

c

No measurable activity.

d

Not determined.