Ring dechlorination of deethylsimazine by hydrolases from Rhodococcus corallinus

Cell-free extracts of Rhodococcus corallinus NRRL B-15444R dechlorinated deethylsimazine (2-chloro-4-ethylamino-l,3,5-triazine-6-amine) to N-ethylammeline (2-amino-4-ethylamino-l,3,5-triazine-6(SH)-one) anaerobically, and, thus, presumably hydrolytically. Two enzyme fractions (M, about 450000 and 180000) that dechlorinated deethylsimazine were detected after gel permeation chromatography of cell extracts. trons is not complete [9] and hydrolytic removal of substituents is known [10-12]. We have demonstrated biodegradation of CEAT, involving dechlorination and deamination to EOOT in the coryneform bacterium R. corallinus [13], and we now confirm that the initial reaction is a quantitative, hydrolytic, ring dechlorination by two isofunctional, but different hydrolases.