Journal of Fermentation and Bioengineering, Vol.85, No.5, 521-524, 1998
Purification and characterization of muconate cycloisomerase from aniline-assimilating Rhodococcus erythropolis AN-13
Muconate cycloisomerase was purified from aniline-assimilating Rhodococcus erythropolis AN-13. The purified enzyme exhibited a novel property in that it catalyzed cycloisomerization most efficiently when the reaction mixture contained Co2+ ion as a cofactor, even though Mn2+ ion has been reported to be the best cofactor for the muconate cycloisomerase reaction.