Detection and localization of a new enzyme catalyzing the β‐aryl ether cleavage in the soil bacterium (<i>Pseudomonas paucimobilis</i> SYK‐6)

Abstract

Cleavage of the arylglycerol-beta-aryl ether linkage is the most important process in the biological degradation of lignin. We determined the activity of the enzyme cleaving the beta-aryl ether linkage in membranes of Pseudomonas paucimobilis SYK-6. This enzyme was tightly associated with the cellular membrane and catalyzed the unique and reductive cleavage of compound II but not cleavage of compound I. This enzymatic activity was stimulated by addition of NADH. On the basis of this evidence, we present a model of the specific cellular assimilation of beta-aryl ether by P. paucimobilis SYK-6.