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J. Bacteriol., 05 1995, 2821-2826, Vol 177, No. 10
Copyright © 1995, American Society for Microbiology

Characterization of muconate and chloromuconate cycloisomerase from Rhodococcus erythropolis 1CP: indications for functionally convergent evolution among bacterial cycloisomerases

IP Solyanikova, OV Maltseva, MD Vollmer, LA Golovleva and M Schlomann
Institut fur Mikrobiologie, Universitat Stuttgart, Germany.

Muconate cycloisomerase (EC 5.5.1.1) and chloromuconate cycloisomerase (EC 5.5.1.7) were purified from extracts of Rhodococcus erythropolis 1CP cells grown with benzoate or 4-chlorophenol, respectively. Both enzymes discriminated between the two possible directions of 2-chloro- cis, cis-muconate cycloisomerization and converted this substrate to 5- chloromuconolactone as the only product. In contrast to chloromuconate cycloisomerases of gram-negative bacteria, the corresponding R. erythropolis enzyme is unable to catalyze elimination of chloride from (+)-5-chloromuconolactone. Moreover, in being unable to convert (+)-2- chloromuconolactone, the two cycloisomerases of R. erythropolis 1CP differ significantly from the known muconate and chloromuconate cycloisomerases of gram-negative strains. The catalytic properties indicate that efficient cycloisomerization of 3-chloro- and 2,4- dichloro-cis,cis-muconate might have evolved independently among gram- positive and gram-negative bacteria.


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