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J. Bacteriol., 05 1995, 2821-2826, Vol 177, No. 10
IP Solyanikova, OV Maltseva, MD Vollmer, LA Golovleva and M Schlomann
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.
Copyright © 1995, American Society for Microbiology
Characterization of muconate and chloromuconate cycloisomerase from Rhodococcus erythropolis 1CP: indications for functionally convergent evolution among bacterial cycloisomerases
Institut fur Mikrobiologie, Universitat Stuttgart, Germany.
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