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Title: Purification and characterization of two muconate cycloisomerase isozymes from aniline-assimilating Frateuria species ANA-18. Author: Murakami S, Takemoto J, Takashima A, Shinke R, Aoki K. Journal: Biosci Biotechnol Biochem; 1998 Jun; 62(6):1129-33. PubMed ID: 9692194. Abstract: Two muconate cycloisomerases (MC I and MC II, EC 5.5.1.1) were purified to homogeneity from an aniline-grown Frateuria sp. ANA-18. MC I and MC II were similar in molecular mass, optimal pH, and pH stability but different in thermostability, and some other enzymatic properties. NH2-terminal amino acid sequences were different between the two isozymes, indicated that these are encoded by different genes. Different inducible production of MC I and MC II suggested that two catechol branches involved in the beta-ketoadipate pathway function in Frateuria sp. ANA-18.[Abstract] [Full Text] [Related] [New Search]