Skip to main content

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