Aryl acylamidase (aryl-acylamine amidohydrolase, EC 184.108.40.206) activity has been measured in crude extracts from leaves of propanil-susceptible (S) and propanil-resistant (R) biotypes of the grass weed. Echinochloa colona (L.) Link from Columbia. Both specific and total amidase activity increased with plant age up to 15 days (four-leaf stage), then decreased beyond 20 days to about 50% of the maximum at 36 days in both R and S E. colona biotypes. Specific activity with propanil in the R biotype was about 80% of that obtained for rice (Oryza sativa L.), compared to 25% in the susceptible biotype. The specific activity of the propanil amidase was three-fold higher in the R biotype than in the S. Partially purified amidase extracts from rice and both S and R biotypes of E. colona were compared biochemically. Both rice and E. colona amidases had a pH optimum of 7.5 and native relative molecular masses, estimated by gel filtration, of 179 000 and 181 000, respectively. Out of six substrates tested, three produced appreciable activity (propanil, 4-chloroacetanilide and acetanilide) in both rice and E. colona. Michaelis constants showed that the rice amidase had a higher affinity for propanil (0.36 mM) than had the E. colona enzyme (1.1 mM). Carbamates and organo-phosphorus pesticides were shown to inhibit amidase activity in partially purified rice and E. colona extracts. Additional preliminary data have implicated peroxidase in the next step of propanil metabolism in vitro. These data demonstrate that increased aryl acylamidase activity contributes to resistance to the herbicide propanil in E. colona weeds. Also, a biochemical comparison of purified aryl acylamidases from S and R biotypes of E. colona is presented for the first time.
Pesticide Science (1994) 42 (4) 281-289 [DOI: 10.1002/ps.2780420405]