Open AccessPurification, characterization, and gene cloning of cis,cis ‐muconate cycloisomerase from benzamide‐assimilating Arthrobacter sp. BA‐5‐17
Author(s) -
Murakami Shuichiro,
Kohsaka Chihiro,
Okuno Takao,
Takenaka Shinji,
Aoki Kenji
Publication year - 2004
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/s0378-1097(03)00933-9
Subject(s) - biology , gene , biochemistry , microbiology and biotechnology , arthrobacter , molecular cloning , stereochemistry , enzyme , chemistry , gene expression
cis,cis ‐Muconate cycloisomerase (MC) was purified to homogeneity from benzamide‐assimilating Arthrobacter sp. BA‐5‐17. The purified enzyme showed high activities for cis,cis ‐muconate and 3‐methyl‐ cis,cis ‐muconate, and preferred the 3‐substituted derivatives over the derivatives with the same substituent at the 2 position as a substrate. A gene encoding MC of strain BA‐5‐17 was cloned and named catB . The catB gene was clustered with catR encoding a putative LysR‐type regulator, catC encoding a putative muconolactone isomerase, and catA‐II encoding the catechol 1,2‐dioxygenase isozymes CD‐III‐1 and III‐2. These genes showed the same orientation in transcriptional direction and the organization of cloned genes was catRBCA‐II . In the phylogenetic analysis of MCs and chloro‐MCs, the BA‐5‐17 and Streptomyces setonii MCs formed a subfamily, clearly distinguished from those of other MCs.