Purification and Characterization of Two Muconate Cycloisomerase Isozymes from Aniline-assimilatingFrateuriaSpecies ANA-18 | Zendy

Shuichiro Murakami | Zendy; Jon Y. Takemoto | Zendy; Atsushi Takashima | Zendy; Ryu Shinke | Zendy; Kenji Aoki | Zendy

Open Access

Purification and Characterization of Two Muconate Cycloisomerase Isozymes from Aniline-assimilatingFrateuriaSpecies ANA-18

Author(s) -

Shuichiro Murakami,

Jon Y. Takemoto,

Atsushi Takashima,

Ryu Shinke,

Kenji Aoki

Publication year - 1998

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.62.1129

Subject(s) - thermostability , isozyme , biochemistry , chemistry , aniline , enzyme , molecular mass , catechol , amino acid , stereochemistry , biology , organic chemistry

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research