Purification and Characterization of Two Muconate Cycloisomerase Isozymes from Aniline-assimilatingFrateuriaSpecies ANA-18
- 1 January 1998
- journal article
- Published by Taylor & Francis in Bioscience, Biotechnology, and Biochemistry
- Vol. 62 (6) , 1129-1133
- https://doi.org/10.1271/bbb.62.1129
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 β-ketoadipate pathway function in Frateuria sp. ANA-18.Keywords
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