Purification, characterization, and gene cloning of cis, cis-muconate cycloisomerase from benzamide-assimilating Arthrobacter sp. BA-5-17

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 sub...

Full description

Saved in:
Bibliographic Details
Published inFEMS microbiology letters Vol. 231; no. 1; pp. 119 - 124
Main Authors Murakami, Shuichiro, Kohsaka, Chihiro, Okuno, Takao, Takenaka, Shinji, Aoki, Kenji
Format Journal Article
LanguageEnglish
Published Oxford, UK Elsevier B.V 09.02.2004
Blackwell Publishing Ltd
Blackwell
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0378-1097
1574-6968
DOI:10.1016/S0378-1097(03)00933-9