The phenol oxidases of the ascomycete Podospora anserina. XII. Affinity of laccases II and III to substrates with different substitution patterns.
For the low molecular weight laccases II and III of Podospora anserina the kinetic parameters Michaelis constant (KM) and maximum reaction velocity (V) were determined polarographically under pH optimum conditions for representative substrates of different substitution patterns. Laccase II showed two peaks in its pH optimum curve, each with a different substrate specificity, indicating structural differences to laccase III which exhibits only one broad peak. Under optimum conditions the affinities of various substrates are determined by their substitution patterns: high affinity for simple o- and p-diphenols, low affinity for m-henols. The maximal velocity remains largely uninfluenced. This study of the effect of substitution on substrate utilization leads to the assumption that there is no specific reactive site for m-phenols in either laccase. Oxidation of m-phenols, however, takes only place at high pH values.
D001203:Ascomycota / Q000201:enzymology*; D001665:Binding Sites; D004156:Catechol Oxidase; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010636:Phenols; D013098:Xylariales / Q000201:enzymology*
D010636:Phenols; D004156:Catechol Oxidase