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Table 1 Kinetic parameters for ZtrLac1A were determined in triplicates, using 40 mM McIlvaine buffer at pH 4.2 compared to the MalLac1A using the same substrates

From: A novel starch-binding laccase from the wheat pathogen Zymoseptoria tritici highlights the functional diversity of ascomycete laccases

 

ABTS

2,6-DMP

Syringaldazine

MalLac1Aa

 Km (mM)

0.4

0.011

0.037

 kcat (s−1)

28.1

10.2

40.2

 kcat/Km (s−1 mM- 1)

70.3

927.3

1085.6

ZtrLac1A

 Km (mM)

0.25 ± 0.01

1.00 ± 0.05

NDb

 kcat (s−1)

14.0 ± 0.3

0.14 ± 0.00

NDb

 kcat/Km (s− 1 mM− 1)

53.3 ± 3.3

0.14 ± 0.01

NDb

  1. aThe kinetic parameters for MalLac1A were recalculated from values measured previously by Andberg et al., using ABTS in 25 mM succinate buffer at pH 4.5, and 2,6-DMP and syringaldazine activities were performed in 40 mM MES buffer at pH 6.0 both at 25 °C. The error in all measurements was estimated to ±15% [29]. bND: Not determined due to lack of activity