Enzymatic Cleavage of the Ether Bond of 2,4-Dichlorophenoxyacetate

Abstract

A soluble enzyme preparation obtained from a soil Arthrobacter sp. catalyzes the cleavage of the ether linkage of 2,4-dichlorophenoxyacetate (2,4-D). The cleavage appears to proceed by an oxidative mechanism to yield 2,4-dichlorophenol. The enzyme preparation converts acetate-labeled 2,4-D to alanine and a volatile product. Acetate and glycolate are not metabolized, but glyoxylate is metabolized at a much faster rate than 2,4-D. It is proposed that glyoxylate is the initial product formed enzymatically upon cleavage of the side chain from the 2,4-D molecule, and that alanine is produced following the condensation of two molecules of either glyoxylate or glycine. © 1969, American Chemical Society. All rights reserved.